SCIENTIFIC ABSTRACT PASYNSKAYA, A. A. - PASYNSKIY, A. G.

• Document Type: CREST
• Collection: Scientific Abstracts
• Document Number (FOIA) /ESDN (CREST): CIA-RDP86-00513R001239420006-4
• Release Decision: RIF
• Original Classification: S
• Document Page Count: 100
• Document Creation Date: January 3, 2017
• Document Release Date: June 21, 2000
• Sequence Number: 6
• Publication Date: December 31, 1967
• Content Type: SCIENTIFIC ABSTRACT

GULIJ, V.Ye.; MAYYLI, N.S.; PASBSKAYA, A,A.
Investigating the structure and properties of thermosetting
electroconductive plastics. Plast.massy no.10:38-42 163.
(MIRA 1b: Y))

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number o( ions in soMicin and to thr 1-5-th poatr of their chup. and too
depends but little upon their raft: the result sobtained on ocintrmted
wkhtbeconclubi(msofl)ebye'sthecwy. Tbeii0vationofthetiectrol)tes

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and applied to computing the solvation of individual kwAs. Atntivs.
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PASYNSYTY, A,; ZOLUTAREVA, Z.
"Research on the Electrochemistry of Proteins-IX. The Exchanre Adsorption of Keutral
Salts on Gelatine", Zhur. Fiz. Ehim. 16, Ilog. 1-2, 1942. Received 26 P;41.
Reoort U-1521, 24 Oct. 1951.

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it.i y ha. I~n im-iigntm and 411%
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11:"I. wt. of IYA.Anyme wm &td hy tA,111" ,,,I 1."J"'*%
d ffu4ion methm] (C.eq. 30, 411,W) and wit, ("1110 to IW,
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A. G. Piasynkskil and T. Kastorskays. rtod. acad.
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591811-Lystsitykate (1) was prqjd. by a modified lkedet
-00
asethod and purified by DouystsovAmiya's nbethod (C.A
7816
O
ll
di
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was
a
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co"issm, usesubrente. A 0.(Y-1 31 phosphate buffer m4n. wa~
.00
isilded to 1. Mtn%. of pli (with a precision of 0.01 to 0.021
'00
units) awJ cOl the elec. coed. were suade. The p1l of 1
after electrophorrsis was within 0.03 unit, of the initial - 00
iralurs. All mesuku ts were made at 2U - 0.01*.
'90
lietweres plf 6 to h I behaves in the Tisellus App. (C.A. 33, 1
21591) &a a hornogmems substance (at least for 1 .5 hrs. at
7 v./cm.). At pit 5 another consponent of I appears.
h
i
i
l
f I i
Th
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i
H
f
s
nc
component o
e
mse
t
m. pa
nt (
) o
e pr
pa
at pli 6 (cf. bbabordin, C.A. 35, N181); the slope of the
0
m"ty vi. pli curve in the region of 11 is 2.5 X 1U -1
This corresponds to the bask pr(nwrty of 1; it is in agnv-
ment with the direct analysis of the amino acids obtained ~60
froml(Abralsain.C.A.33.78311). P.and K.assume that
~00
the ousts. lytic activity of I and the max. aburption t4 I
by sensitive bacteria probably correspond to the H (if 1. ;00
of isstle"tclawlyrriatied toll. The diffrOrence bet wcen
I'**
I the 11 valuird 6 and of 10.5 (Aldsiton, W&Td, and FewtA4,
C.A. 39. 16W,) is explained by the diffrrmcv in the con - zoo
Stilution of the buffers used. Look R. Nfarchi

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4131)UMSMS Wft AMPODIB= IMMY&WO. A.
and A. Uuk*A-. J. Gm. CAw U.S.S.It.) 16. "-W
(IM) (in Rusm"u); d. C.A. 17.1 XMI.-Tbe 6dook
int wimi dad. for tgg albunilm by 1:11MOM with 4 coacus.
K
S
of NII.Ch'S: lee
Siv the imetbod of buNtrim talapbortsis at 8 comm. of NH.-
C.NS. The bo-kc. point of the prote4a is shifted undn lee
the influence of NIIC%-S to the acid sW. in mtmst to
the imionic point which is Wdtrd to the &1k. side. The *00
0 0 Wt d both points is Unctirly connected with coma. o1 .00
NII.ChS. The electrochm. data we pared with des
dima mWo" ot"aremsts of binding of CNS ivas b
go m1bumin. The rcsct&m of egg albunda with NtLCNY.
tul Imoo
in coar"I to AsA, Is chlimcitmind k7 The Fr*dmi- 000
o00 tantly ovLadmorplitmoltbes0t; the muels"kesth"It
J is of mcoadwy impartm* mA decreues with Increased roo
~Concm.cfthtsmlt. Itissupposed that the C.NS&dmwp.
tion act: rs an the by*owbm noom at tbr protein
mob. 11. lnbmtdm id emda With *Won aw"ide.
IM. 99&-1002.-Tbe dimwn. cowls. w3d she content of 2 go
AAL!j
otytic Voups (on mol. hub) wm cakd. lot castrin.
dais wAy be used to cak. the isolonk point of pure COO
castin with good apremat with expli. dols. The cakd. as 0
isoiODIC polat is 6.0; txptl. value 4,11. 71irstion of Canis
ist 9 castims. of CAiC3* (0.002 to I Af) was used to do.
the istjoink point. It was shown that under the sajou was
6 shifted the " skle. Diniffics of
of Cach The pow to
CaCh by eaveim 6 predomina tly mol. in ebuiscter; owta-
thesis is meomdw7 in importance and decreases with in
creased tows. of the sidt. G. NI. K06DUPOff
V'r too
4V 10 't'. 7-.-V -q 1A I I a a v a W 01 1 a a 31 0 v
I* w ;~11010 A
16 Lj
OTfs, 0 0 0 0 o1: 0 0 0 0 0 a 0 0 6 0 9 9 WJRALO- *000*0000000000

OL -----Wcmmm
ago P.
is MA a X w 10 w 3 a v a IP 0 a
-,A.*
T'L-0 0
go 4
111"Whou"y W pool"". Kill 1"MY0114"p.
0* .0 g:!MW v"" of VW0w. A. G. lla*jm%kd.
go c".7U.S.S.R.) 16,1440-WIM)OR V

go cf. C.A. A7,2WI; 41, 2628c.-A summmy d ft

o P. wul bis cuilabamtors &M d* 0 yrs. an d* ap-
-
UtIthir dmbk4a
er
tb
i
d
k
l
*g
go m
w mam w
st
cas
t
y
k
p
I to the electnebem. proj*nift of pmeim, Is
0&
go
00-1

Goo
too
go*
coo
go$
Soo
b u a Av so is M, a, #11 ;Flo; -,I-ma 1411WO "*?voodoo 31
IN
6640*0100*0000006*

00 a
00
00
00
00
00
00
410
00
0. tt 04 Its *ill oil
#W#GUS Also plPeollefles m"S
0 Jl) 9 4-pt
thetIlk" of below oaae"wnwn I no
vistalwoment r, %, C-4twAsys dfv1L&-f;-
All ~ Ilk V, ck- it SSR I J`b. 711., 1T(FwffFr- I'll -
0"Off"I" Ilwa M, ..,% ff. . 1). As"we'll" LAH1111
,,, t I ill Is! A, *it fit 44
I 1 4 -,1 -- i4lmlof %,Lit ill i, v %j4Aitm.,f sit 41clod. 11, The
maleculm wethl ilad the psllydiaWyAty of rubbw from
4iflusion mp&wvmtnb A C N.YesAR sow) T %
AlAv. 116kf NS 2A. f- (*.1. 40, 41,401 Is 010
, A I) it oJes" -,olvw .I wark-.14.
L 61-1,14 h~wu 9 the lot%, f.4 11%. Imoth
P Tht, ratio 0:10, ill IlAr ,Urfi. Ill diflie,s-vt
fiml (Iw 'Imisdist'l I"iAtb'"I ar.1 boto the
IN- urw -ft-havitw imlv% Ilwlatim 484141-1
I, A Uirfiql1v A Ow Vtk-
z 101, aml 0,I), are I'm a twitfol
117, 1 17; 141C a n-plot(L fixturs) rulpher 0,401.
I -~ 11 *#).1 1 Is, Lw . IlAlt Ural I UWArr IN-01.41 I;) airm
11,11 1 is, Kq, 1113'(616, milet I 6w a 'Null. Isivillyl "Ito.,
1 1, 1;'.. all-I I CI; 64 4 1410 lAvitlyl fulAwl ff.-I
- 1K. troul4wim-f 3,". 11. &fall 1 37; *10 I'm a l4b
vsi,vl rulAx-f 6316118. vl,rw limmumuner A.4, 31. &AM
.,Ikl Tlw A( vat"" 4vkNI. Irml 9 af%~. of
1(91,ttlf. "IttvIl MMSIN-f flUll (he &IknV %-akk-S.
.00
VID
.00
we*
as*
Ce
see
0
Z! soiv
GO 0
40
w
I 41rr r~
or.. o An
0-61 do 4"V
Its 111 41, on as
oppovi*sfl up 411 Donal us a I Is A
0 0 0 0
001;000000 00 0000

004
902 50yaom of mommistortlyt" and comprvevibility of their
A. G. l'asynskil tKarpoy Inu. I'llys. Ctwm..
80146M.
a is .
Ma4wow). J. Pkyj. -Clsro. (U.S.S.k.) 20, t"1-401
00
09 (1916)(in Rumian).-Tisr inlenw rAmnprruimi o('W'j
0avrest Around Vacts li*WIvc4 dilloic MCA. Ilet'stsw (W%
Plivirw4rirtion gives riw to an -incomprmllible vol.- V
(osprummed In mmols. of 1br Mvml PrY Irsol. u1 tolult).
09 4111
00 0
IT ~RATWR CLASSWICAMM
slow 27VISPA"
ljpbaoj~ *AP o.- clot
-
114 15 A' 40 131; I-P n' N' a' 91 s' M a a It 00
o 0 0 0 *1* 0 0 0 0 0 0 0 0 0 0 0 0 a
a a a a 0 0 a 0 0 0 0 9 0 6 0 411 *-&A
J01
40
ttt'i'6j;! s)

To cut. V. time vorksc y Cl m tim, sob". -
-
-
0=7
~
M 1-00

94 Ustawmad as bric.. (
W d. Com.
S
.
2,
4
=
41;119y, P. raled. from Mom vdarmy valswo and
merpared with list tell pirtmilsiMil ef The pm w4wPl. 1-0,0
77W 0 01
sq. stsins. drrrrlm~% altnnbt linearly
;lwvs the *00
cown.. g in wt. %). increases. The lowest IDOMW
(
't
he biXhrst g Y&IMs 4,1d. art. F"P.. for MeM 43.23
' 1**
Ne unit is not drills"I in file orisinal). PAA: Im 10011
12-M, $.00; PrOll 41-7N, fi-OS; ethylk-m glyed 410.73,
11.41; suerelse 0,10, 18.34; AcOll 42M. HIM;
HIC(hil 41-49. hutyrk- scid 42.20. UA2; 6-
0141411
bulyril. acid 42A.1, 7,K?; vai,-ik will 4S.W. 2.02; nsan.
dr;iv--scill 4"4. 1.9d; oulic "I 42.M. 4.16, lortatic
-tsciil 41.j 1. 347; citric acitl 42.78. 4.01; amone 42.M.
73W. ures 38.91, 14.73; Slyclue 42-31. 4.0 1; mA alanine
43.99. Vill. EIOAr lowers 0 of "tam from SPM X
W-* to 81.67 X 10-0 at C - 30.7; and & 28% Win. of
4.
:mylarristrinsertonch".9 - W-73 x 10'
9'-
U1
bo
t
8% mobs
C1 CJI
n
i
68
I
i
f
)
.
.
ll
s
e. an(
a
.
on
n. o
G
lv
butyl mik. in heptatir have 0 - 115 3, MA, and V2 '9 x jj of
I "
go
10 - 1. rrsp. From thme 0 volurs V i% taled. It is found
that 11 Is fivilependl,ni 4 the tcnglh of a mol. and is ap- Cgs
pros. a4ditive for its t-Asr Irfou 0. RVelry Off grmp
'
V. SO*

contributes 2-3 malt. of if I
XJII antributris
'( to
; C(
34.:C0 2. and Nit, I mol. Fr(ml The fiterilturr it is
ctlachadrd lbat the airlphyde Vmp bimis 2 nsols. of )1,a
In org. sWvrj3ts V is almi 0.21 mol. The effect of a pulair
group on 0 is about 0.3 to 0.5 that of a uni-anivaltsit ekc-
t"A"e. Bike"nall

.10" &"Inv
11CW B11151 am a., is-1 too
d-V
0-0
M
V
g all D W 9 -1 is is
0 3 9 v
" Is 1 .09
0 0 Ole 0 0 0 0 a 0 a 0 0 0 0 0 0 0 0 * 0 0

PASSYNSKIYO A.
Chow"try - U99021W welot
'DeternimtIm of Molecular Welgtt and Polydisper-
isity of Rubber Frcm Diffusion Mminwommts.," A.
ftemynakly, lab ~ Colloid Cbm~ Xw76Y Inst, Pbys Chm,
T. Gatmakaya.) lab Haercuolecular Structure, Dwk
Blockew Inst, Acad Sol USM, 20 pp
*Acta. Mwelcochimica MISS* Vol XKI, So 6
OcMutem molecular veigbt for tbree rubber samples
ft(n measurements of diffusion coefficients and - -
isymetry of particles; calculatem "disperilty
ioceff Iclents. Notes close correopandence, between
.110001'rads 4 ftp 194.50
PJA 54T33

A _11
ISO
PINVOCIIIIIIII dw ofewitrift mall.E
'"Of
On Slip &imvpwy betwoom tho 1wicink wd Ike ift-
1110 On 1111b=40
V,
A
ft
pA
VPtkiU
0*
i -
.
.
-
_
,
ca"Pi. Pf"Id. mialf. no.
96.1c"kays
*11-1 T
.
.
-
11
d
h
4
I
A
l
mi
-
ir"
5
an
off t
n so
rex a0mimin adlimbril oil a
"fill how that thr'lifictirponcy birlwavil the i-orkir. 611.1
'00
t.wlic Imitilts perlii,its even if) Im.1 little %4".. of the
protein sod cannot lie amounted Im by the effect ol buffer 00
6 SAIII. 24 -Ugggrited by Timiiiiii. This diveirparicy may tw
explAill'a by the face th4t the portidev of thii, protein ore
t
b
h
i1
f
.0
ac
eco
acc% t
ey c&%
gfishWAr of m4n.. while on inter
y 0
dMAWFI-11 And ildi4drd The Chiblifir strirtme is per- see
J rootigh to tile i"11% of circitolwl". still Its l"Hen-
'11cat.1r
O ,
I lontemc I it rat illm whral t hirrillollyllaillic equil lostimill"l, Zoo
goo lie Jo,tributi..u .1 the ionq procteds in the normal wity
"tilikv thi%, fit electiukmetic mewturriticilits upon which
h
d
f
i
i
i
f f
Zoo
om o
on o
rec
e l
m
tat
-wive are IM-1. t
m"willi-Ill of Ow ion. i'l-ol, it,, rJohol'..

,
r
00
.Vl..t
loa'lwat" tile... I., 1.o. v%trill C. K i
00
00

t I goo

ILI
E:st
Slim
WAL Ll 900TIAl CLASWKII"
!!_T'LLW(
0#4009 d
it,
-
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u Is AT 00
" ;
0 F F
v it I
q S
Ir
; to, In tv is a a w a " a a if a kWh 3".Ank 19 FM 0 It 9 '1 9 111 9 dl 4 3 6 1
444
1
0 0
e 0 * 0 0 0 0 0 0 0 0 0 0 0 a 0 0 0 4 0 a 0 0 a
0 0 0 0 0 0 4 0 0 0 0 0 0 0 0 0
o 0 0 0 0 0 1 0 0 0 0 0 0 0 0 0 0 6 0 0 0 0 * 0 010 0 0 0 0 0 0 0 a 0 0 0 0 0 0 a

9
A fit Is 011111111111,11's 16 1) R W 13 M 2 10 V AT All a 11 4; U 44 0
A A-A. 1P, IA I I I , A -b 4 . A-#
004 P: - M A-15 .p ter'?#$
Oes, -
Ole j
A. D. Pasys" md V.
10 C Gatowsbays (KWPM Ing. rb". Chm.. MOMM).
or $af vixcwt
we tow to amabs tabb computit =.
ft "Mm. Tbr m"bal b
vahabb fm bbs. Abld m-vmg am uInwratrUM. -00
008 savrHO ZUBSOU
008 00
=00
oleo
00
.00
e9v 'coo
coo
cee
see
.00
No*
We*
too.
11 "
$*Moto -0 4110.4 .1. 11. .14.11 a" It.
- r- V T1 A I a pw --- ir -10 -9-jj -a Ie W1
w IN AT OD As a 11 KW a I as end
*0 go as "0 non
0 0 0
0 0 0 0 0 0 0 0 0 Ole 0 0 0 0 0 0 a q 0 a 0 0 0 0 0 0 0

UM/Skdicine Pmlolllin. NOVA~Sc UT
YAWCInG
"PIWalcoc hemical Mcbmime of the Action of
hoijcIllin," A. Paey'nekiy_ T. Ewtorskm7a. I&b'
CQ 0
GO Of fte Chem, Inat of B101 Propbylaxle of ihfse,
time, 12 pp
"Atokbim" Vol =, no 6
Direct micrommomtric studios jr*vGdjp&d4"3"
zRiam~. *by-pp
.,I]- aura"_! Tmajumesm
2b
that'Part of the ned-maism of the action of'
pWclllln In dependent an the action of t1kis
substance ou anzpwa in the bacterial calls.
62/hgThB
USW/Mdiclne - Pamicillin (Contd) Bor/Dec . 47
2041illabed lImIte of oxidation-reduction patea-
tials of bacterial calla (Stapb7l. aurams) =d
expl&:ined aignificance of conditions
thle proeoue In the calla due to penicillin.
Maltted 6 Fab 47.

~201
0 to a 0 wwww-W20
1 a L
J
4 a I
r
I
1
__
j .
-
_
W.
. A__1_A_ M ML CL 0 19

all

wesol m6 of rubwr by 4
I
4
P
I
0 r U1
00 MOSM01110011. A. (I
and 1. V. Gah
aswoAk
Aayo K&n.,v 11141. Phyi Clwtll . Kwmw) Kish
C*4
d 1'
k
377
1W7
l
30
9
S
A
C

00 -
).--
tw. am
#c
am
.
wv
.
.
(
.
4.5.4 10. C. C. Davii
I
J

:0

go
0
A C. 1. I_& 4
00
09
06
90
90
00
'go
00
ww
PO IF
too I
00
00
00 &1jALtU%&K4j LIfIRAILON CLAMPKATPOk r3 10
00 ---
k; $*,Dog -d a.. got
I . -)-$-I "T. _T _V-71
u 111011100,9 w Plitt 0 d 0 0 11 6 M III tat It a A I Aftl to IWO 001 N 64,3410 30
0000000, +tpo a wee,

Jan 1947
Solubility
Fluids.,- Compressibility
"Solvation of fion6lectrol~tee and, the OcWessibility
of -bbeir-Solutl6na.- A. Fa6synmky,,'Khrpov Institute
of Pbysical ChmIstry., Moscow., 16 pp
",Acta ftelcochimica UM" Vol XXXI., No I
compressib-111ty of solutioni to shmn to
-ALetsrulpe the subject solvatlon. Meaeurments are
given of supersonlo velocity., ocompressibility,, and
-.0oliation of aloohole., organic acids., eadno acids.,
eta.,, In vater anil of etbyl and a*l acetates In
acetone,, at various concentrations.
RA 26T61

-W
1,"
uljwr)4 It's It JIM -1. As
00
Is, 17 a a a 1114 a Of a
conwilswilft of tkwdm3 actaftm abd
tu faniicai
00 calliaAda.. A.G. 11talaynskil. At to am. U.N.S.S.
~
1=4

00 cf.
.x atiVirmIrt.
1
The nw0voti 0l datt be salivation ol di-Mml roan
P
L
it
t
f1w rorn1wr"
y of 1wr Militia. (voled. frin"
l
t
role ol Ittoilialatim W olfrommk, wavrit) vkos tralml it) tkt.
-ANIVIIIIIIII 44 0 1)(1, 44 V1411114111. 111 hImb 0WO. W. St VIIIi-
11"llits air givrif I'm av)atio I" Ititte woll-I
(11 VilliOUS 1111 ~ JPA'f`tyk-WIjIJj4tVV,
1
1 cthyltvilullow its met-toile: Ilifforvllultstc In 4-41111C.-
go 11411elle; natural "1140m in CS11%. eclat and C,111; vi"Y1
rtilitwr In Cilia and CCIj. slid ~wlvjwene (C.1fcl) I" .!all.
atilt CCI.. No significam difirwrtacr was found betwern
00 th~ .4valims ut cou'l.f. of high 0 ... I I.. .". .2.
pla"Ig Cowl

&$O tL LITINOCAR 1L.111FK--K-
'ka., ".0,
-14f
-0 - r It -4-1 A a a
&a
AV to At, 0 to to 0 Ad N a 4 11 x III a to ft KO A I via
o 600019 0 goo** go o o 0 0 0 0 0 oie 0 0 o6 6 0
a 0 0 0 01:0 0 0 * 0 0 0 0 a 0 0 a 41111 0 4111 0 0 0 a 0 0 0 0 0
-00
Zoo
111141111
coo
WOO
so*
lie
0

I I PiAlkrl~_m -
oe"
1. -is -,.A-- IL 1'. a It,, 1,a1 I- SO so 'A L1, It 'k I
00
00
00
00
00 1401w# CA Alobuhn ptelftn' V Sy" them4z of ptolein
SOL* substantes in tho globulin CondittOn
it I.AlIal.1, 0 1 'A""I'll

.1k %I I wG'. ( 6". /,Nt,
56, ~.,_
cl .1. 42. ;17V.'i- I$v ,( dw,lll-
%nh pl'.111.111w. thurt 'itil, SIT, 1.1 P.1, VP41A.-
11milli 111"I -I- A."It ~Nllll .-d
go 110 L'(I( .11,4,1 IN 11o

AAJ
f It I'S I Is, I'm I W11, I t. j -
I,vf% H.-tv lital If ~ Kit

I'S
I, tit . ..... fit, 1,111 110m
Au.,11111int 11fillffs art till .111110t.1 m.$- -1

Offat-1KAL LlIttAll,tif CtAjjl?;(A1M&
41' No* n n 11 4
oie
IS 0 9 0 0 4110.411 0 0 0 0 0 0 0 0 0 0 0 0 0 0
00
-00
coo
100
t:o
_i w _i- A- fl
,w o- 4 . ~ I
0 SO 0 0 9 0 00 0000 e 41 a 0 0 *~,A
**go* 0 go 9000 *see* 61

~L--bbor,
Jun 47
"D8GtrtWUvn D18001virZ of Vuleanized Pubbart 8 Be -ogmlldnt S, Tar. om, t,, TuV=jdyP
FbaCov Inat Elm Mm Techp 1. pp
"DDk AkOd raWk ~ZS14 Nov-, ~or" Vol VIj 11o 7
ADDertm thA+, vu1C=3zrU~;.-; should be considered proem In which main fouture jo
fonati-n of spatial structme for molecular ollmlna, conneotod in operati,,:n of
vulmrdziM IV forcon of main valoncov, Demwiboa procoon of dostraotive
d1onolvina of rubber, undoubt&lly of Crest in,-ortwm in tachnical procosson .r
refurlAnhinc; rubber by diaoolvingretw. niustraw witin cz-vom.
~4 COW.

TO

I L 6 4L U A a v P

The reactions of proteins with nourltct'OlYtes
ganic electrolytes. A. G.

so vank

0o . . ..... It X1 I...

A 9 A L._A
or Vo
Ve
'90
!too
0 &$*-ILA MITALtURGICAL LIMAIL0111 CLASSIOAKATION tb*
oil AiTakcr_ IS,
u IS AV 10 'a-T --TtTf
OPOP41 nails plan 4101KW;~,An set** PWO00"Of I VIZAPO
0 o o 0 0 0 0 0 0 0 o 0 0 a

UM/Chadetry - Gastin Iky/Jun 3.948
Chemistry - Deformaticn
Ofte Deformation of Molecules of Gelatin In Solutim
During Changes In Their Charge," R. Chernyak, A.
ftsynakly, Lab of Structure of Albunins, Inst of Blo-
obse, Acad Sol UBBR, Moscov, 3 PP -
OKollold Zhur* Vol X, No 3
Rq*rimental studies of the relatimship betvaen the
d1scharge and configuration of the gelatin molecule in
buffer W nanbuffer solutions. Submitted 13 wy 1947.
PA 78TIO
40* 78TIO

PASnISIUY, A. (-,.
Paspiakiy, A. r,,. 'Tiffisi,)n un,i -r-derular weight of iinear
11 In Uie I nvc!j 1, ~ f,a -,i iris in :.ne ~ i o! 1-J )' r- .. . -x-
r",)I!!C.Lll;A.r p i ; , ~; ,:~- " 3-70,- - '-)I - -
-ral, I
rloe, -,,,)w- L~ i , I - :~ : . I I , ~. .5 .
-%. 17 Dec!nt,ll)er .)53, (Lt'-- -'s ".hur~,ai In, !c S*,%tyj ..,. ,,

PASPISrm., Ax.
22350-Paaymsklyp* A.G. SovrewnWe fietody Opredeleniya ~blekulyamikh Vesov
VyigotDpolimemv. Vyisokomolekuly" Sojredineniyap Vyp. 81 1949, S. 14-23-Bibliogr:
S. 23
SO; Ietopial No. 30 1949

-0 -0 AIA -6 A a A-** -9
-
-
-
1 If 4,0
09 1 .I q
by
1
eassims) a Apo
t
oo

c
4')
C(1%1
It
1
4
1 -00
:0 .
e,.
,11
111 fil
-Mill 8
.
* M urrA vmt 4.#12 dikl.5.45.4 fAl
x1r. aw"I ',
LN, and li.74, and S.#4 irsp., aml thfic (d 1,
4n mj~ V Ac,*s*ll,. 0.3 .11 anifirie, anti 036 M pyrichur
nit MANI, itij rj,ji. A thtwy tit thr Ort 1 1,
tit miv "-. the hih .4 th,, I.-hit h-iiohl
-4.* 144661 h. I b., .44w. . 1-1 tit Ill. f0mlv. voll"16"ll
..I ifi, Ilv.... hill tl,,~
I'd Llws~lw. Inia.te. thr -mr,htmtbK. 1. it.
so
11111 Ali. il il li it di it 6 it il v, i
coo
coo
go*
see
800
1000
in,
-00~
M-T190, softie me"N Nome -10 v=

The dovolopinval and 0a present staft of Cbe physical
cheirtilwy of probLas in U.S.8 9 A. 111, Asoyn4kil
I tv#hi StR-remewRal thol (Advuncrs In h1olcm MG4 )
is. a," 44011401 Review tif the wark lsrqelr f(W the
J."'t 13 mir. G. ~l K~4.11-47

FASYNSKIY, A. G., and PAVIOVSKAYA, T. YF. (USSR'
"The Mechan-'sm f the Oxygen Effect in the Irradiation of Proteins."
Rerort presented at the 5th International Blochemintry Confress,
Moscow, 10-16 Aug 1961

PASYNSKIY, A.G.; VOLKOVA, M.S.; KOMAROVA, L.V.
Effect of radiation damage to the nucleoprotein and lipoprotein
interfaces on the enzym reaction rate. Radiobiologiia 4
no.1:29-35 164. (MIRA 17:4)

PASYI-:SKIY, A. G. and CII J-INYAK, R. S.
"Adsorption of Non-Electrolyte Molecules by Proteinsp" Koll. zhur., No.12,
pp. 46o-66, 1950
Translation 9006479

(21)
PAMSKIY 0 A. Rilect of detergents on the Bensillylty of Proteus ")Sul$
xnd,E%*jkbis toll towaid Wilt o r. xa~vwikuya
avitVA. PaSYMAkil, 001114dy A . NM SX9. R. 73, 453-
5(IM).-To each of a series of physiol. solus., 1)11 7.4 +
0. 1 was added one of 20 different co3n. detergents ho coacn. -
1-2%; the soln!;. were htattJ ut 80* for I hr., cooled. fil-
tered under stcrfle conditions, and mixcd urith the pure
cultures (of Protrus ruILarl's (1) j411d B". COU (11), re'ultiug in a
0.05-1% (approx. fmal concu. of the detcr-
&cuts. Thv ~cu%%Iivity of Ott: bartetia was dctd- by a
standard titration method u5ing the physiol. sohis. Without
detergents as blanks. The threshold of dic sensitivity of I
toward ptnicillin was lowered by 13 detergents (even more
than IOU times by Na p-hexadecylbetizettesulfettite). The
role of the detergents was to increase the penetrating ability
ofpcnicillin Into the protoplasm of I by affecting the cell ruern-
branes. Pcnicillinase (not affotctl by detergents) In It
eliminated any effect of detergent on sensitivity of 11 toward
antibiotic. E. Wierb;cki i

Dolorsomwe of ot9w at this kwass 78*14 b
@*MOM of of 41111bottom. A, Q. "Ma :2 V.
I"him. DW, Ak". Noal S.S.-S.74-JR-8
(IDW.-The tensile charactaistics of wool and link kMtj=
AM Muscle Protel" were examd., using Various saw. for
inimersion. At 22' for wool keratin tbt values Were.
in ilia, bysteresk imp (in % of am Go t be extension cum)
43.0. Work of extension (CaTrw to 3D% relative extension)
".0 If 4.1), 36 and OSS; in 5 Af Urea.
43.~ biu.0-114r guanidine nitrate, 25.5 wA 0.78;
wd 1, and U. IA33; ~iu 11 %% SVa
I s'n" 4 )
1~ '.4 in 3~
0 I'l er
k t
7" 0 31- 05;
01 0~
- i)l; .0,00
~7 62W'O Wt. is' 40. were
"Aum tesud reduce the wwk of extension wW decrease the
orn of byMovau kxv except for Na hydrosulfite. The
'embatisom. 020W the I&M. weaken the bonding between
the Various regions of po!ypeptide chains. retaining the
wriles-4 lWa. In the cabe or hydromitfite the disulfide
%Wm we ck&vW and the work of exteasm drops sharply.
WMIs ame lintemb Imp am incleas" owing to lbe pm*M-
it OF "remobi"tW, of the attrisdive areas of dir Irml
LA. chains. an event impoobib3c in the Ut category
. With rat sartorius muscle in 0.9% KxCI
aD% cattaxicia ttekinique, it was fouad that in
dim ~Woft is Aboost 100%. In
phate (ATP) the work
6 Ar woo Oarip
cd c2ftsmAcis was but 0.7"A and rnWuaJ extension after
3-4 bra. was 16-17%. If ATP sob. was replaced km="-
attly after rernoval of ked by pby%W. sobi., tbt contraction
to criAW sin tutvk Placv, but with uru solo. residual ex-
let- rrmajocL The hy%tcresis loop um was 02,,, fog
Physm. Nacl ;;i 67-74% for ATPsnd u:ea subs. &a.
of ternp. dependence of stms in The fiber, in 1&.60- jnjcrvW
&UDwed computation of the entropy FaCtof Fs in the Work of
Wtuskm for the mious fibers studied. In hair keratin
this was 11-9% in 11.0. 14% isi SJV urea, &Dd 21.2% in by.
drosuffite soln. The latter was 344re for wool keratin.
IICDM the entropy fairtur rise$ as the Amu of i,fud., or ea.
tin chains art freed Imm previous hnkMn. In ionxh
fibers. studied at 1640', tbt tzuWy fKiot in The BgIns. of
urva or ATP 6 rather high, not un 3D.4L)%. Ilgoo.
&Ibu7ys (C.A. 41, 8PD4t) id. of c=pkWy eoardk
Mechsaisru Ed ISIU-1, 'Unt'action is iworTftl; This is also
comfir-d by a-rsy irimlizzlions (C.A, 44. gQ74c)
G. ?.I KO~61.'H

C.A
Swpdm of nmilioew" c4 accolrebwYles by proteins
A -G. 'I'" iskd and R- S. Chtmirak. DoAWy Ahad
j~.%h S-S.TR 73. -,. 1-41 ["1).- -rbe fechniquit tof equil
thoilosio thrutish colkodinto membrane witio u%A to %fully the
~-w Ptkm of WrA. ituankline nitrate. urethan and 1110 (m
human owfut" albuilull. V-01hub". %",I h4if &fill wtvill krra.
tint. at 3 4' Me etpuitim vouss"tnt Illo,
w 1,4 xm by % siro-kil som I PA "wis I t' .4 33. -, OP I
in tak it. 4 tour n-u-1.vimlytor glowin I he t-ult..
Sma graphically. had tht, 1(0.11 t4 (VivivAl [Angimut
th"ms with a vicAr amir of min. which g4w if-A- ~Alut~ if
friax. ad"pluou. The extent of hydratt,"i t). 11 -4) it)
I'S k"Attull. 0 5 0 65 Illf SkAllilin. Atilt W7M a a 6w A-
~muituk t1tra rracl", m%tv 0 Ci, And 0.341, su,mi
dine nitraft, turflowl, OM.O~',S.
MW totiout 0.3. Ctik-u, ton snotAr bamq show. orplout .,I I
tuirs unit tvr 2 ounino acid midum, While othet nouckttfo-
,Ytrs give a 1 3-4 tiolso flor %It protrins and 1:8-10 (ot
RIM)l urwli~ C' NI Kt-L.J.41
i olt

PASP-ISKIY,, A. G.; Zasypkina, P. S.
"Slactrometric Titration of Penicillin"
SOURC3: Voprosy Med k^him,, Vol III, pp 94-101, 1951
W-24414., 31 Oct 52

USSR/Cb=ixtry - Proteins X&Y/Jun 51
Immunology
Conference on Proteins - Proteins in Industry aad
Agricu.3.ture (20-23 December 1950)," A. G. Psaymakiy
-4 "Uspekh Khim" Vol XX, No 3, PP 382-385
Reports on conference on proteins held by Dept of
Blol Sci, Acad Sci LUSE vith attendance of over
700. Papers delivered at conference we e concerned
vith structure and compn of proteins, their dena-
turation, their roles in photographic, plastic,
2AMber, textile, and food industries - S. Ye.
193TIT
VM/C.hMni try - Proteins (Coutd) 1jay/jun 51
Brealer's paper stated that resynthesis of high-
=1 protein under pressure restores haptenic pro-
parties in lst stages, then completely restores
antigeuic properties.
193T17
>7

PASYNSKIY, A.G.; ZASYPKINA. P.S.
Electrometric titrntion of Denicillin. Vop.med.),him. 1:94-101 151
(MIRA 11:4~
1. Lnboratoriya fizicheskoy )diimii Vaesoyuznogo Tinuchno-igsledovntell-
skogo instituta no T)enitailirtu i drugim nntibiotikAM, Moskvp.
(WZCTROCHEHIC.AL ANALYSIS) (PENICILLIN)

Resittim of platim *Nb &at talstilms. A. C. a-
and A
to, I lill Pbl).-,TU deviation himn milifilivily 4 pult-ti.
tioniftliv T111.1.1kin r"IT" 4.1 millo. of 1410w 1041111 Willi
lon"In (Kalitimut" $*tit at"t Omit ell 1 1% O."Illied V., I~
a measure tit the drom of Inletarlion of the 2 mil.limm,
The Tattle tit deviation It m1w tit lilt I A. I v, pt the ittirlec
point. rew deviation Inrytraws With micidlfwation While In
&1k. reav it rmbrs a miss. at about pit R 4-P.A. At pit
10 the pure tannin birAllix miniotinteJ to 0 11 x 1c. retail".
0.2-0.4 S./g. 7U invite, polut of The "An is bimul.
lislic"Wy "led to pit 3.6 by tannin and to 4,4 by col rat
Notiolaroff
ay

Mentkmetrk study of roactim of platis witil tamins
A. Q--SVwfn*0-4no A. llui)ova~ Doklajy Ak,&& vshk
S.S.S.A. 76, 7Ll-l4(tR5l)--Alk*litoetr;c tatwitm curve
cif mixed gelatin and tannins differs from the IndiVI(JU41
curves of these %ubmancts. Plaut tannins give drviazu-
.1 all pit values. but the difference is leut at pit 44,, ~
in&% t* found treat pll 8 S-VA Mineral tonijuji Alui gi%j
acvialionl: Cr alum gives cowntiAlly neg dr%lition up In
1,117. Ikud a jun deviAtion at hishrr pit viluch ttsrs with till;
Al alum gives a characteristic Mileviion near pit 5. nme
values are Closs. to the sn"O of tonnallon of hask, %All of the
mrt4l, The ralk) of the difler"em ~n olital"cil to the i-u-
,umption of alkali by the tanning OubstAnct Alone MY giv'e
4 ineiAtire of the sult. of tannin bound by CeLitin. 'rhe
,multi to obtained an somewhat higher than those obtained
by IvAching mcthWo, Possibly with Cr Arid A) alum, the cu-
,,rdination of gelatin takes plam at the IxAar nonionosenic
llrouq'N koll. ptptide. etc.). G. M Ko%otapoty

W4-
of djulmomwily co bonds in proMp
=-A -4T., r M-A plvty .46.1J X464
K t4 Tokinill't
And tf-ICI J( .4 19, 14. -') that thr fr" ciwfai" of all
M~Iidr hnmi, Art %be ~arnr is untrnAlt- in view of the
rspli tlata of Iluffman (C A ~ 37, 107141, and o1 LeVY And
.4Wmlizasky ((.A 44. f*)14r) Oth" re-vill IlIfTsIllyr
twarang m thit prvAA"n f. rrvi m I I P Da"Phy

KOLESNIKOV, G.S., otv. red.; AJIDIRLUOV, K.A., red.; DOGADKDi, B.A.,
red.; DOLGrJPWSK, B.A., red.; YENIKOLOPYAN, II.S., red.;
KARGDI, V.A., red.; KOZLOV, P.V., red.; KOROTKOV, A.A.,
red.; KORSHAK, V.V., red.; LAZURKIN, Yu.S., red.; MEDVEDEV,
S.S.) red.; MIKHAYLOV, N.V., red.;J~,kS"
_5KIY, A.G., red.;
SLOND-ISKIY, G.L.0 red.; SMIRTIOV, V.S., red.; TSVETKOV, V.N.,
red.; FREYMAN-KFUPENSKIY, K.A., tekhn. red.
(Carbochain high-molecular weight compounds] Karbotsepnye
vysokomolekuliarrqe soedineniia; sbornik statei, Moskva,
Izd-vo AN SSSR, 1963. 287 p. (KIRA 17: 1)

I;-
49
tam
tth M
~
jut tftRtim
47 'n 1
f
'
o
.
C
ts
'
Vo
u tea
and R. S. Cberayak. DAW
7 v
01
~
Ak
6Z. -
.k- . 0. 3001-4(1951).-Ile purpou it
wasiodet-lbeprop&valueoIx thewlvii~
t1nve.411MI-factor
In -
the equation (I +APM.

R ,
,
,
'to
bu.
Is used tr, compute the xtbttive change in the vol. of i
lin. For ruols. baving a loose structure, x - 11. or
t
structure, x - 113; And, lot the nori-IlowIng ellip-
=
D2taorstbeureadenaturationcifsemm
Albumin, tx; alburpin, horse sprum plabulhi, and gelatin
data on the solvzoozi torrretion und the
Acanacyaltheine"ure.

Lion includes the effect of solvittion. Forglobulins,theip-
parent effects a elonpi3on Are deld. by the 3olvation force
of urta. For Selatin vith high natural asymmetry, the
solvation force of urea Is very small. Actual elongstioh of
senint albumin (after deduction of the solvation correction)
even in compa~atiyely coned. ures solas. Is About 2.0
Scrum globulin 13 very little r-hanged at the same conca.
These data indicate ilic high degree of 3tability of the pro-
tn In 3tron
tein globule t% g denaturants. One can abo ex-
pcct comparatively mnall protein deformations during the
wusl pl'yslol. conditions. This conclusion fully corre-
Sponds to the new x-ray d:ita on structural analysis ov the
const. InIbelimilsof thezone
of St;.Ml4Y. This wability of Couriguration b PIVIMbly the
t.)u5i&iilt)iL3tabiliiyiiltbeirbiol.sljo6fkity. Iti3powbIr
that the grrater stability of the globulin configuration is
tird 3jp with thrsMial rokof this prottin in The Joiruilion

of antibodL-4 dw:ng immune rractiluns -whese it
With p1htin. &.13brous I)Mtelt, ft double t1ougation was ob-
served in .41 urra whkh is x Jar lower cozen. than tar a7bu-
spins. The rigid TATU th the XtIxtin PWS. apwently Poe-
Res cousider-Ably Ligber tetibility thin the ugbt)y ended
t*ti L3 the Itiscondudedtbatfurdenatu-
ration, 3D-40 breAka d the !,eyvulhundred H bowls wbicb
mfist In a mol. oY ftmm 1lobulln wilb ;& inol. wt. of A8,MD,
.~rr suilicient. AlthotVb the full unwinding of the 2nol. at
prottin during dumturation doeq not proceed untandItion-
ally. the Oonzat)w oI the protein intA. in tb-- dem. of the
dpirep of densturution aftar the Intuducticol of Wea and
the brzAlking 0 the minSiod no. of boads Is greatly Jae&
anthi. The rate of the processisca1ed. for bone strum a)-
bmnirz 4ind 3:j,)vn clearly %he "true" chutce In *symmetry 1
-A the 1,ratein suol. (nit" the 2olvation correction hns been
upto3murta,the
tlungAtloD is about 20% aud, apparently, Is not related to.
the brmk)njr of the bawr ?)ob-a)in structure. In greater
of urra. the elongulign 13 sig-nificantly 2nodified, al.
though It does not attain coinpNe unfolding -of the chain.
DaLa ar,, presented which %bow the intermittent ebametrr,
cf&.e beiceenaturation prates3ol thesplitting of thestruc-:
2uze of the pr,~ttlri =61. W.H. Fitzpatrick

-rote ins/' kjloziaistv,~;
kozif er n t s o ,-o:: ~x iria, V. L.

WHOUTINA, T.P. [translator); PASYNSKIY, A.G., professor, redaktor;
GRISHCHWO, Ye.D,., rejjFktor-.GX2jMWbU~,' Ye.S., tekhnicheskiy
rodaktor
(Amino acids and proteins; a collection of articles. Translated form
the linglish) Aminokisloty I belki; abornik statel. Ferevod a
anglitskago T.P.Rurokhtinot. Pod red* t a predial. A.G.Fasynakogo.
Moskva, ltd-vo inostrannot ltt-ry. 19529 394 p. (MIaA 10:2)
(Amino acids) (Proteins)

V=X%c=i8tT7 - Proteins M&Y/Jun 52
%'haav of Yom of molecules of Proteins on
Damtamtion With Organic Substances," E. Chernyak,
A. PanywIdy, Biochem Inst imeni A. N. Bakh, Acad
Sci LIM, Cbair of Gen Chem, MATI (Moscow Avn
Techwl lust), Moscow
"NoIlold Zhur" Vol XIV, No 3, ]pp 205-211
Ca" ca the assymetry of horse serum albumin and
Berm globulin, humm serum albumin, egg alb=JA
sad SaUtin were carried out after denaturing the
substumes in solus of urea, guanidine, etc., and
ccrreat4d W the magnitude of salvation detd forwrly
b7 the authors. Gives various methods for caleg
solimtloa correction. Ma alb-Ins, the appanat
stretching of protein mols is caused'to an eqtAl
extent by the effect of salvation and by actv&l
.stretching in globulin the effect of salvation is
fi~rmter, and in highly elongated gelatin paTticles
2ean tban in albumin . Actual elongation of..zola
U 4d follows, in ascending order: serum globulin,
serm end egg; albu-In, gelatin-

A.G.
Chemical Abst.
Vol. 1.8 No. 9
May 10, 1954
General and Fhysical Chemistry
Change Of AsPe of Proteld rpolecules during denstu.Q,
bi Organic substances. R. S. Cherm-ak and A.
k-I B
hem. ITISM -5
M mg]. IratiNT-i-ti-nuT
T~ I P52)( r
P.

USSIR/Chemistry, Colloid Proteins.. Jul/Aug 52
. . Radiation Effects
"Modification of 'rnfrared Spectra of Proteins After
4.
Irradiation with Ultraviolet Rays," A. G. Pasynskiy,
T. Ye. Pavlovskaya, Inst of Biochem imeni A. N. Bakh,
A
,%Cad sci U3SR
11 Kollold Zhur" Vol XIV, No 4, pp 239-249
Measured infrared absorption spectra in the region
2.0-10j4 of human serum albumin, equine serum globuliz~
gelatin, casein, and cysteine after denaturation by
the action of ultraviolet rays. Shoved reduction in
Intensity of some characteristic lines and
225TII
demonstrated connection o.' infrared spectra not
only with elementary groups of the protein mol,
but also with the specific type of coiling of the
polypeptilde chains.
I, 225T11

IY
Chemical lAbot.
V0.1. 48 *;,,
Apr. 23v 1441
Biclogiftl o"stry
Afterstion'of th& infrarffid onlffadla-
flon whb ultraviolpf. AA. 0.
skays. couOid J. (U.S. 14, X5-73(1,1,1? 1n!1.
trarjsIaflw).--&e CX. 46,

P-V>YMXllt A. G.
30
Dqormation of ketatin of hair and wool in solutions of
organic compounds. A-G'Ila and V. 11"WA-hilla
i k"
N, Bakli Im.t. BiLocheill., I "M
W.
khf~pl~- -M-Abidy 7-of Konf.
Vy.tokomol-kul. S~~ipieniyam 1952, 21it-7; cf. C.A. 45.
684e.-Measurements of tensile strength, tile rc-lative size of
the lipteresi,, rinK, ,in(] of tile temp. clependence of strain of
hair and %vool kerativi in soins. of urea. urctiwa. detergent.;,
salt buffers, And Na dithionite %vurr malle. Tile ivcakim-
ing of intentiol. iinciaction (s:tlt. If. nad nonpolar bonds)
leads to a decrease in the tensile strength and to an increwse -
in tile elastic proverties (,Aim of buffers, urea. gliftni4ille,
urethan, deterl;tnts), while the rupture of the (lisaffide link
by dithinnOr heith tensile slieng(h and vh%fiv
prnp~rtiex. If. 1). No(IIIAL.-

nartims ail
(Acad. Sd.. Moscow). DWAN"i)c 1 17, IRA-UAlijul).
cf. Anwm, CA, 40, a "cin denatur-
alit. don not affect the oskatioll-reductim potential 14
%ilifilydryl cmpds. The tam of asitiation of Sit mrispols.
i, not depentirAl on the oxiiiation-greftetion potential.
CmW. solw. of CO(Nifth will analloguot, w1starim hastrij
the oxidation of simple SH curolods. by ak. 11 P

PAMNSKIL A. 0.2 NEMM, A. M.
Laboratories - Apparatus and Supplies
Laboratory fermenter made of glass. Mikrobiologiia 21, No. 5, 1952.
Monthly Lilt of Russian Accessigns, Library of Congress, December 1952. Unclassified

$24 771.5'1 547.962.9 541.183.23 67S.024
TAMMca" d Gelatin with loorgaak 'ftrWgg Agmts. A. POPOVA and - A.
IsAromy, 1. Appl, -Chem., MY.S.R., 1952 25, 18-22-1ft quanlifl~.s 6t
ifuja~~ and chromic oxidc3 adsorbed bygJaNa from potassium and Fhrorne
&IaM &Ad from potassium dicbra=to have on determined from thodiffere4ice
between the potcollometric curves obtained by tilrating mix1turci of gclst)n
And the tanning agents *ith alkali, and-thme reltich would be arib.-cd at by
addiq the curves for the 6tmtlon of ft compincati with alkali scimramy,
It hat been caliblishcd thnt tbc polar, non-ion icnigroups In jdatin play n
coritideTable part in the co-ordin;tivn sphere cf 11 -c a uininjum and ch,-umillm
atowt bound Dy g4latIn. Ahf.

PASTUSKIT, A.;BIA)KHIM. V.
4"~A
Diepl&C*Mnt of isoolectric point in proteins in their deformation.
Doklady Akad nauk SSSR 86 no. 6:1171-1173 21 Oct 1952. (GLKL 23:3)
1. Presented by Aoadamiclan A. I* Oparin 3 September 1952. 2. In-
stit%Lto of Biochemistry imani A. S. Bakh, Academy of Sciences USSR.

PASUSNIT, A.Go;TALWO. D.L.
Change of amino acids In protein molecule, in vitro. Doklady Akad.
nank SSSR 85 no. 6:1361-1364 21 Aug 1952. (CLML 23:3)
1. CorrespondIM Member of the Academy of Sciences USSR for Talzmxd.
2. Institute of Biochemistry imeni A. N. Bakh. Academy of Sciences
WAR.

Ti SK
11 aot5lCl. The :i4er-lipi? Wr%'
S.0im. %kith P.IX Kit
Cut % " In m A mu-bom 1, 1,11. 17-4, i1h %I ish
rillvv ill thr, tnill;1m, 11t, it tbu lri~
ri~li-l MI.-I. umbil."i Sip jvrOaMr YwIll" 1, 14 b I It.111tt Ot,
,b-!pr ul ill,! fitiAi,* cmit. Th, cone ba~ t,,m : 'wlhitimi
;y! igid cinrf-~pmflillx to p), ,12.4 tint) 'IX
The a x-rileling fifrnt~nl Earik in t311. tilrdilitil-ItIl 6.2-1
in thrir-oln.
to ISr irrmi" 4 hi-ilit-iy] b!7jJJnr,,mmt pirt,104y oi-ing ID
the .10~$k'Ztral;Ct C-1 IFIVW C31`1)1~%)'I gitmpi in Me ~,hj. nivinj
to tbE- 11:Mtolyih Of W.1-1-Irt.Mll On Illt! PIWIDIP167)
h3t thir *lit. tl,*s trit vAm?ain rmy Olirr rmul. cip3ble 44
bir ilit i)6~. vi )7)rtj. of fy-,~e nrolf-d to N ing thr %,)Ill. frinn pil
7 to Ill' I 16, b the im. of rniMmOts of arill nert--mr) it,
brin, Ittic 1,11 Lark W7, If" G - 11 - f, WhttV V 13 the W. Of
im;MmoIr-,7f prilkillm. "is tnetliqd iq reprotlikilile within
a uremi ri wl IvirtiriMn itulloted tljr ptimt,itire #J still it ollrrs opt
ii,it I ty p- it% I w I lit Wit 1, %v Well c,41 IwA m 40t. t1t .4-1, Id Ir
itM I 1,"j its Oir adio?i M prili,ilin on I-n-It7h a0d %shith a
wrtr pill dii"lly conniciftl vv)tli the biol. arliv)-y 0 Imid-
antilay

fie subject and the Fdntlpl~a of a Comme in taff5w
chemilstry. -;-AAi P. Va rer. v-,%d B. A.
OjQrnwv
should rmbm-e "t-41oldAt mlns." (which am thlermo-
flynamic-ally tcversil4e) ml "Milvidal itotil" (irtevmihlo)
lita O'v6d d(Saimicm of lrov-owl. will. and wftcrv~wpic

]PASYPS11Y. A.G.
Second principle of thermodynamics in biology. Biokhimiia 18 no.5:644-653
S-0 153. (KLRA 6:10)
(Thermodynamics) (Biology)

OboalomaAbst.
Vol. 48
Apr- IN 1954-
hoidetry
Problms fn i~ z frolcin inblecular
A G.Nsym%Lil n I V. 4 Ujfftkhi Sotrrmmr.4
Diol. 36. 23f,-All lfr~a, - T. F. 8-

Tho union of n4tiblatl
CS V'tth tht) I)ACWNI cell. A M,
Nc1r;ml. alld A, G, I'mynskiT(Alf-Valon, Vri. !~,_;Warcjj
Ptrfornll grith pmkillia, wt.,ptomycin,
grwnmidin, CrYthfin. and lysatymr, wlug t1kroc6ccu,
py'v; var. ~ure~, Ok'rlicillin-wusitive at 0,02 "its/ml.)
L-garls (Pe II'leiffi R-resistant, at M units/mL)
rwilson
W; the Irst, oti The antibiotics tested fell into 2
gToup-4 (1) JV16011141 find q'TCPt0jnyCin, Of R Very JOW Aatl-
biofic blmling urvkr alld (2) RvItibiutfes of the polylvept;dc-
prutchi naturt which 4iclude the remaining , , IG 9,
*4 antIbi-I c
The degirc of bivlini; of which by tht test mganims teaches
5-1()C/,d of 01C. %%.t. of' tile I -)wcr by
,wteria, The binding p
--a, _rtf of-the
the-5pltiltivc Id '. -Wtude
antibiotics Itstcd %vas prictically Of the sairr. mL&
"d the depec (if srusiti-tY C-r-0~sIstfInCe AV= a function of
the spe,~~c wl"Chmliml of action of the antibiotic In rela-
tion to w.1ch fictors as the biohern. properties of the vaTIM's
I=tejial :straius order diricrtut growth conditinns.
B, S. Levine J

FAM~ ULIX, A, 0. and BELITSZi,, V. A.
"The structure of the protein molecule", Uspekbi Sovremennoy Biologii, Vol. 37j.
No 3. pp 358-360# 1954.
SO: Tranalation-"95, 19 Aug 1955.

MM'd by A V
S ) i" )S. :i.") '11, cf 1 1 -2
o3 1)
111I.I!N'-- ILI tlh!
I I In Alt-
rp~ of .-c;-1 !,
,dt r i , : 10! 1 f
1 1), lim .2 t 1 Iv. 4 t '11
In"I " I t 1v 1 ru y, I n 1 1), of 'trvill-
). - I! ~is t'vl'
Irpt im; o t rt- p t ,n A;'; t 1 1;
CA 1 !11 111 ~l i 11 C 11' i1' a c d I-C I Li !I I I

Mir
A. G.
2;'m
ut
q ro!
-ITY t. r,r(,[i3:cT .1 J.f,tj ~;~Ii riviop'I" I!;,
La
11,tta! fttv.
it
'Vd (bz.,
zl,t~tA-I lIv (lie IJ,~, TV-111"W] iiII.
,fi
rt-'V5
X.Mvi
It ;11~3_:~',14-1 f!tut
rVitr'.( afa(~.'
occ
G_. 'J.

PASYNS-XIT.~- A G.
Quantitative determination of the rigidity of globular protein soledules.
Soob.o nauch.rab.chl.VIMO no.3:28-30 '55. (MIRA 10:10)
(Proteins)

i23
ALTZRATION3 Of TIM ULTRAMLTT AND INYRARZD
SPZCTRA OF ALIBUMIN BY MUTJON. T. 2.
PAVIOVOMYS Rkd A. 0. Pa (Bam biochemical
wom Trar, -., 305 19U) Jaly-,kvg. On
RIMMIA)
Altentloss. of ultraviolet absorption spectra in Um 340-
to 340-n~p r"ge *1 bumn serum Albumin, seraw
z1bumis, SwIttla, sad blood strum of a bDrse vith x and
ultraviolet radiation of various doses And tM lntrxM
Absorption spectra of loiman serum sibomln =4 gelatin
radLaticivivert %yevilgated, OLY.J.)

LIPATOY.S.M.
Comments on the paper: OThe subject matter and princIples of a course
In colloid chemistry". loll. shur. 17 no.4:324-327 Jl-Ag'55.
(MLAA 8: 11)
(PasynaklY. A.G.) (Vasillrov,P.S.) (DogaMdn.B.A.) (Colloids--Study
and teaching)

ly
i.4'Tha t9ed of ultraviout and of Rantgezi lirradistiola'an
solutions of proteins. Al. S. Volkoys and A. 0. Pasynakil
(A. N. Dakh Inst. Biochem.. Acad. Sci. U.S-S.P., Mox;iw). I I
Pilikkiini)ts 20, 470-P(M)'.-Nre preplit. of buwan wtum k~n
ulbiamin wtre atalued electrophorctic-ally and dried at low
temp.; horse ierum globulin im obtained by fractional
pptn. and d&alysis. Amino N %va3 detd. by 7tbe Van Slyke
method and changes in soiy. by the Ale. magulatim method.
Nonirm,diated fractions were used as controls. For the
,dem. of the quantum yield. to 4 mi. -of the protein min,
lrradiatcd by ultraviolet rays, I ml. of ale. wa3 added
the mist. centrifugtd.. J'he sediment was washed twice
with 1: 4 ale. soln. and dried to const. wt., which repre*-ntM
the amt. of.irradiated denatured prottin. 77he addri. of
I mi. uk. to 4 ml. of nouirradiated wramm fractions failed to
produve any turbidity. The Intensity of irradiation was
2.3 X 104 erg3/cm.*/sec. and on the exitire surfact of IrTadia.
tion 9.6 X 106 eirgs1sec. The ratio behveen the
~)f 2% ,1, ?uantity
Mi. .
.of denatured protein iassuming . human
serum albumin clautain 1.8 X 101? protein mols.) and The
gi-en no. of quanta during the irradiation per:od (assurning
the fty. energy quantum of 8S X 10-12 erg) rrprr--.e-nts the
av. magnitude of the qu3ntum yieM, c46 in the interval 250-
mia. For an &q. serum Albumin solo. 7 X 10-6,
and w;lb pbospbAle buffer %si t vynewli;a 15Zhei piolim
conct; '0 - 5.3 x 10-k =IoW irr-IjiAlr-3 tjo~ aTA ;-f,?
Ita dets. tbc extent of protein dertaturalvm.
will, irwrease,in the protein suln, Concri. life ji)(1rarr !'-,) il:1
vl%cos,ty tinder irradiation Is lessened but Yipetific vj%coliy -
'%;_ r" trinains const. In bitsid intvivAls i,f vt~nvw,
m a relation Littly to The denatured pDrzim, of the
protein. Amorg the physicochem. changes are an incxra~.e
in vis,-wlty and turbidity, a luivering in the threNbold r1
beat m-igulability. amino aci,is by the VanSlyke procedine
and cj)tiW rotation remain unchanged. At the i_~*rltc.
pciint il,=t t' Pears more sharply drprvss.-d than
ura on a=
t the' Of Values. albrumin is more easily irraillated
-by ultinviolet ral,3 than is serum gic-bulin. Denzaturation
of protrin solias. by ultraviolet liradiatiun in The presk-m-e of
dettrLimis and urea showed an increase in the valur c,f '7,
and in the pre-lence of Na caprylate such values dtvte.%, d;
a decrease is found with phosphate bu!li:r (M115 and pli
7-0), The ;., Is g,=ter in scrum aNimin than in N-luin
globulin. In the case of P-butgen Iff2diation the eXcet Q
30,0W Y. could hardly be dewted. Measurable ervis
wemobtrined with 75,000--101r. Scruniglobuliawajincue
mistant thin se-rum albumin. ArainoNandcptic-alrota.
tion mnained unclianged eyen after 2)(),0W 7. At 101 r.
:37% cf tljc protein rtnuiltut naaljeciH. Otl;rmi3t t-,c
tffec!s of Rbntgen-r2y IrTadiatiDu of ser-urn protein fraoitnis
ran a paialltlmurst of tffects with that Of UIL-avi("m It-
ndilliDD. B. S. Lryiu"

1i
1
P
1 i
11Aj 11,
t hloehei... A,qd. Ski. V.S.S.R .
1A
j
j
~
i
;j
h
2
o
W IOU). Cf. C.A.

MA e. "MAWil Willi u
ltra-vialet, tuys W." (julle wills a i
PRK2 "pot 220v.,3.HLuvV. Forinudidtioli,wiltul.*em

~-vd r4% Petri dirJae-4 0.2 cip. In diam. to u. depth of a Sam
9
V
tit aLnjtppcox.vuJ. (420m), Vari p6tes were covered with
cellopZwte awl the nohim. kept cold with ice. The irradia-
tiou di~lawe was :IS em. fronk the axis of the Limp
i
CC41 blitmity Willi ilitervab; of 2W-= toju URM
.3 X to$-
CigAq. tra./scr., und irriidlut" dtiration wile 10 mill. It-
radiatimt with R6019,hi ruys W" dont by ZL short-(Ociil OF
Aube of V~ kv., 6 itia., A -Q.dttW,&ud 10.20 Y 10W r./U".
"The it-tadiiLted holti
wtu Phiced into a Plexitlass cu and
T
cooled by rurmine 60. 1`fik-ktje.,;s of will. was I
,
C".
V.xrt W the expis. was conducted with Rbalgen therapeutic
tubes (IW kv. utkl 8 ma.) with uliticalluides; und itradfittion
ljjtcj~ity 4jXl-700 r./mIn. !rradkitinti of the solit. was per-
forriii-d with paw filter at u d6unce of 14 cin. in a cello-
tube- Detitils: of priccilures used in the
_ittli'li" with 11'e 1j;Xl- Slid nuckoprotchis; art! outlined. Ir-

hatit the thyroid tLutd. aud artific4l Ittlits.
'01 Priteiu Willi NA oleate and rilorluck-it: acid, teNts were
mide for ehatigra In VisrCitity, SpeCUOSCOPIC Ubsorr)(Wu,
eke I "tx-tk pteptrt ice, Luid others. Theoltwivedthrelh-
T
ol,d (
irr"Litida activity for lipoprodoin (by (lie isolojAc
macd.iA) was dew. at IW r.: for uuclei)pmteifl by the viti~
i
cotity teNt) za !Z-50 r., wbith b;
le Value of
'
vwt.v"u kb~rvutitmii- The stabili
1y of lipo)iroleilts t/i it-
mliat"t 6 r"weir thim that of pure protthis. Tile six-
ulity "f is hilker th(wit that of tilicpriticitis,
I* the CS.'e af mtifteLil IlliXtS. of ;~rejteltlq. NN, Mid 1111CIti,
atido the Ltmr C.LXett 1, btabilizing effect ou the proteins uuder
itradiatioat. In (he irrudial"i of Upopro(cias uiul uuekr~
'Peateilie there is obaerved a 1-21%, selm. tit complex cons.
psnetits. A emmideruble degree of delwilymerixatlais of
uuv1.s+u,u." and i higher degue of liolymerixulititt of
,aucleic az;A& appears iiii a tusic structural chimSe of these
*ub6t=u*-&u.&firrudLitinu. Tlieyeuuliitol)liiiiLtlitulicate
'thAt uuc"qs"cin I-, Will. upffoin, bkxk tegments bound to
ow anather by'~ucteie mcid.
.~evitte

X014ARDVA, L.V.; PASYNSKIY,A.G.
Aggregation of protein molecules in reversible denaturation.
Ukr.biokhim.zhur.27 no-3:330-334 1955. (MLRA 8:12)
1. Taroslavskiv meditsinskiy institut i Institut biokhimii im.
A.H.Bakha Akademii nauk SSSR, Moskva.
(PIIDTRINS.
aggregation nf molecules in repeated denaturation)

4Z,47.?.T I
F P~ Y m .5 V__ I
U-e%4R/Biqlogy - Biochemistry
lurd 1/1 tub. 22 -32/51
"Authors Pasynskiy, A. G.; VoLkova, 11. S.; and Blokhina V. P.
Title
Isotopic method of determining the denaturing changes in albumins
Poiiodivd.
Dok. Ball SSSR .101/2., 317-320,, liar 11.,. 1935
Abstraot j
Experiments showed that the denaturing of albuminous substances results in
an increase in the chemical reactivity of numerous functional groups of the
denatured albumin. The introduction of a new isotopic (S35) method for the
study and determination of changes in albumin due to denaturing is announded
Some results obtained with the new isotopic method are listed. Four
references.: I - USSR, I USA, I German and I Belgian (1948-1953) Table.
Institution Acad.,of'Sc. USSR., The A. N. Bakh Inst. of Biochemistry
.,,-.Presented bp Academician A. 1. Cparin, December 24, 1954'

MWBiology - Biochemistry
Card ---1/1 Pub.. 22 37152
Authors Pavlovskaya, T. Yo.; Volko-va 1.11 $0 and Pasyrwkiy, A. G*
Aft
Title Change in S35,mthionine blood-serum, bonds during denaturing by
radiation and heating
FeriWiC4 I Dok. IN SWR 3.01/4., 723-726., Apr 1. 1955
It is ahowni on the basis of experimntal data3
that the denaturing
at 'Serum albumina by radiation with ultraviolet or x-rays. by
and
beatingis accompanied by an Increased absorption of the rarkod,
methionine regardless of whether the serum is pure or under the
effe at-of the microbe factor. The increased adsorbability during
denaturIng was found to be due to the liberation of new active groups
which become saturated by each other. The nature of such active
groups is described,, Four USSR references (1948-1955). Graphs.
Institation Acad, of See
USSR) The A.. N, Bakh Inst. of Biochemistry
Presented by s Academician A.Z. Opraln, Jantiary 14, 1955

WYMA %Y P~ G-
V 1~'OP-Jlmc* Ill hydration
furs of ths Medl roteln
A G!~, I oil And tom
M a hem 1.1a -, Amylaskii nnd
kkV Akad & ' ..-Aw &- U - J* R. El,plner
0110i ZA , onk .031. 1-1,S.R if
..b Ur. -11, 53(194 1 3
serum "Min, ?a Albu ii)-Hydrt'lon "I
JaItthod of cra min, and Vial' 3
Of Prt~" - deld. by th "' was " rtd""by jhj.
SuMbolaic Waves In the 301 e rate of p-pazation
0' all 3 Protein, hydrtj. ns- Itandin '~Tavt Jbtthod),
poln 0 ZiSC3 oil botil
t fshown graphical]
oil bot
b side* oi tj I Y); In the PH the la-ki ,
je atter be by', of about I a
const"S At about 0 3 0 / ration 3 xubsunthai;.
and 3 or ta pZlp glhlti- nd 3MM albumin
St I~ t hYdrAt'
0*109 to 4% ZL-z 11 curve of gelatin Is
=-Iption Pact structur' and MIT fieziale
Shoyrs MO - 'n the PH range 4.4-9 a burmu, 7.Zjcbuiin~
significant b4
'an Y'
a h EO in hydrnti~n Temp. lqwd.
se
~.b u-
'W Iar 0- b-oslobI4 ad
I by 2D- dans. show Almost Me
dep, Iml;
0

PASYNSKIY, A. G.
"Stability and Instabilit., of Album-rous Substances" (Ustoychivostl i
y of the Third All-Union
labillnost' belkovykh veshchestv) from the book Trucl
Conference o C9jjg&d-Qhemi , Pp. 391-396, Iz. A14 SSSR, Moscow, 1956
P . - -q:Lry
(Report Elven at above Conference, Minsk, 2-1-1, Dee 53)

5 Klv

DDrr a o1 def Iml-Ail't
v 01 pr;*rf
-
1jt'9 if-ft;. kit. 0SA, 1, W-15 Y'll, Not. Rhin-l"
*
i
N50, At),-ili. No. m
c5_
rhe c~L%ol-tin;l Of Ic"'tive clongation qj
'
1
ci;l 111~4' dvp.~;lding cn tA;-crl0s
L'Bi-pac;idal P26
ldic repulsion ol lt,"Xk~
l
rc folic,,win;, forinda for the rigiday rn.
cltafg.~3. Icada to t
o1 tlaB mz'~c"Wn
in. 1,4,1mm.
'

E-1 i-37 X 10, D" III, 'X (x-xIY - 1)1;
il X Ual b,
~.hcre! it munibc. of cha;rt~, ti-a thc inol=u1c, S - sutfmcatca of 2::~
C"'i Ar3d 1), ITe 5111-1,11 MiU 11~11-aXCS Of 1.11141,40fil;U]
ratio c'f d0ormed
tl -nt~m. Caicukl o
rvc~prucal 4:4 1-11% hick ti, n
of I, v-ap 4,i~~d on d.~,( a d Seri ved ifroiz ltt,~ f a, I,.- e (i -I c Ividing d atp. obtz ; f) cd
by t1w ~wlhorj on rha-pe, -~ and bydratioil of ItInrum :trtldl Obilmill

16; in -
[1), end egg alburnin 111, of different I)H, For I : n
1-01; and %;.jt*h it - 16-4; E 00 k-./m--L. I-or 11: .v-;tl) pll 5.0
5-8 6'-in - -1 -05) 1 i ii. Tmm I, dwras
ci~ldr bolli I
.
r (Olmatiom ~ ThA
Prewlice of
and .11 vAth mppredablt dt,
rcutral Wts Incroas-3, B. The valuts of E obtzLncd arb approx. 2
-
l
v
l
ast
cm
tha7 th
f
ubber
h
d
l
f
d

d
o
r
o
an
axe
t
r
Or
em o
r
ym
1
g
v rjwd ;,o tho cu-rczpondi rig va] u c5 for yamfd zin
agr~.wnat ol es d
.
U'S~xczyNs
l
!
f
as
3c3 o
t,7pc% n)

-imam

^oter cas b tho Inaditition of.
tlire atdotl of towo subsLm
14rotein solutt-ow. T. 11. Paviorikaya and A. G. Pasyriskil
IN. BaLkh Irst. Ac'-A. Sci. U.S.S.R., Maxoty)..
Jalloid. Zhur~ 18, A t5 --ub-
irgir than B (z is
stwice D if tr for A ia ton3iderably L.
-toncri. and i ratc of rciacti~,,n with the radiwJs pmIuced by
Irradiation), It (cs)A< (c.) a, A dotsmit pr9tect B, but B
proteco.A, Onr g-rgg albomm cwUlned 5,7 mg. 511 (as.
eptinuft) Mum, 11A mr. S11 aftcr Itr3diation with 150,M)-
tBritgen5, and 1,2 Otte ii-tadiation with 2 X 10* "p of:
ot 0.51`,~ cyrtc bit ti 0.6%
rach radical prhd aecd by
-with the subs
ty 500 quanta rtz~nccl trate. wid "'t protec
Oun affordcd by cy.,;1,6w !in(i aworbic teid was de to their
'vely Wgl at all cqwwl c, had no pwtoc-
rel liti 4
tive al~tiou; Its r vlut;t be Arnall. Large excerl of pyrotar-
trati! N necdcd Vi piotect c-%IalAse (Fc~---~bctg, C.A. 41,
11111 11, Mvwed that ainall aints'. of catalase pro-
-htni", tr
fectO vyrzt~uvlflc a6i. Atriviling to ShcL
'T~.Tj abont I pL
(C.A 45, 2 ), , ~rt rf gluco~c (1) wall mcdcd s)
h4lf OIL- &-ilruction a I P;~lt of Illethylene blue (11); "till
now Drm--d 13-t44 lay 11 w-m-dem-naweaed, -knittilkA of
cj~d #.
sis for SH ill pf'w-bi ill the pm-'ence 0

PRSYP4
~~Wmys~ L 0. BaUovs, sarl A. G.- puyaws (.k, X:
JIM lpt, Illochem.4 --Acad, SdCU.S.S~R.,- Mozom).
U 44 k),-The tffftt a R6ntjjtd yartl
21, 7W
*crc Kiuijed o the hpoxidxi4 cl ioy 11%tr and an pao;6c
ficid ILE4 w OwAple It% -pure (aim And 13
the mmultuaft-a fit-,latka 4 Inixt. at HwACM sm- and,
cmterm, Tho ImRalvadon 07%) dwit lQr &y llpqxMio
i wm;l,&4 X I Ol r, and to Lola. 6wOw r. In slobi.,4 100,0
102 r TM
luutivatim of lipoxk~= aacwtd 4t 40
olltutim of 11POXIdala procce&4 In -tjjc form of a
0 the (Sdllwzil~
iact leution, Oa the b"9 of *.a rmilts
IrAc."WithA IjMxlUV the trio!. ut, of thia czy'Yeac Wm.
to he ~20wl it WA8 demoustratm fu. the';w's ol
ur
-ed th
;me The inattlyatim o! thC
h
Xj (". P~4cutymlc oF-(dMj*A Ot, she suhstmtft of
s3 a moJt a lvw-clo-m- x-my IrMIAOU" were W
Eploo'n' ~d4
gm -,Ate in tlle&,smvt-,; Of UPI& me%Wum,

PASYNBUY. A.G.; BLOXHINA, V.P.
ft
lusysintic oxidation of ascorbic acid in an open system (vith Rnglish
summary in insert). Btokhimiia 21 no.6:826-833 N-D 156. (MIRA 10:7)
1. Institut blokhtmii iment A.N.Bakhe Akademli nauk SSSR. Mosirva.
(VITAMIN C.
fermentative oxidation in open system (Run))

/Effect of lorAdng Yadbtfi
H. V. 0, Dolisova'. and A. U.
(A. N. Bakb Ulmhem Ipt. -146~ow). , LOWY
Ahad. Xa~h S.S.S.R. 110, 6W-6(IU5K-T.iPoxIdase ac-
tivity was detd. of saybeansw ticated with x-radiation in fig.
f te with dosage up'
soln. at vefrious ars. or tn' ft AoM t;
OIDDODDr. AedvItyd;c4I*' _s tolarlilunkafly with dose c4
Md1atG).'- Thus, tht luactivition apptarg to be a 61ukle-
set Pbenommon. ~Cal&_,., thomij flint the probablt tuol,,- -
w+ unit of tho cuniiie iv IMOW, estd. Imn kuown d, aad
On
-the trtmpoIxted voli r4 1 M XjO_" MI, rCqUIT,'d
fu~r I
va
tion pbegointam
ifugill tsfq, if the J110, an.
i1ther vNa witicent,
------------

MWQ INI P _--O -11Md i P~751

V 6mution of ascorbic acid in flow conditions. A. G.
Pasy-nskg aud V. P. blokbiam (A. N. Daldi Blochem. Inst.,
Moscow). Dokkdy Akad. Nank S.S-V.R. 111, 1293-4D
(19M.-Sim6_11tancous aldij. Gf.Wns. of ascorbic aritt and
Hs% in the prmn.:E (if ptPruxId4--,-- (front fiorac-radish) to an
app. provided wit-ft a seinipcTuivable mernbrane in contact
Ividl Constalitly flowilig 1110 Waq exalild. as to the rate of
oxidation ofascorbic acid. The khlutics of (lie reaction are
examd. and the kinetic curvei are sh(,wit. The systun -
'Eli alAlIty to cuif,
shows the typical eazymic Wt iuvior wi
prnsnte extir"ie-s of concti. of Me reacUmB and to !Aabilize
itself dynamicaily as the resclapts are brought in contact.
The statiouary-state stabilizati(m is itt.-sinAle, with Oianges
I
of 7-10% of the transfer cutil
in the synAtm
at riaujin temp
.
~
,

PASSINSKIY, A. G
"Enzymatic Reactions in Steady Systems," a paper presented at the
InternationalSymposium on the Origin of Life, Moscow, 1,0-24 Aug 1957.

"The Primor-, Fo--mct`,~- Ami:-.-
Electric Discharge," ul. twit. Ti fl--L-,~,jt;--:iaA
on tle (:rji:llr: )' Life,

'emicol li-,E;titutl,-- .~.S WSR,
A. , Barl, Biocl,
"Tlic Charge and L)L,,,'L)rmaticT-. of Prtlel: molecules," o pi,-per sulum'-to.' -,t
the S,.,mposium .Iacrom~ Iccullor Cliemistry, 9-11 -';OP 1S,57, ".1c .

Lil-
~)~c Ii.tcr:-zi r
em " - V~, ~, l: .1~ ~ ~ , s T F
0~1

Y1q S'K_Z'k~ PR1Kti6VKD, F
24(7) PHASE I BOOX EXPLOITATION SOV/1365
L-voy. Unlversytat
Nat*r1zly X Vaeacyu?.nogo s"*shchanlya po apektroskopil. t. I i
Kolskulyar.Wa spektra)-plya (Papers of the 10th All-Union
Conforence on Spsctr,3acopy. Vol. Is Moleoular Spectroscopy)
(Llvov) lzd.vo Llvovakogo unIT-ta, 195T. 499 p. 4 000 copies
printed. (Seriess Ites PlzychrM abirnyk, vyp.
Additional Sponsoring Agenayi Aliademlya nauk SSSR. Komlsslya po
spoktr*okopil. Ld.i Jazer, S.L.1 Tech. Ed.i Saranyuk, T.V.1
Editorial Doard. LA:vistsrg O.S., Aca4szlaian (ROU. W., Deaeamed).
d Pl
S
i
th
t I
k
c
A
ema
o
ences,
yalaLl an
Neparent, B.S., Dontor Of
Pabollnokly I.L, Doctor of rhysioal and Mathematical goltnces#
s
d M
l S
~
r
th
ti
t
ema
c
ence
a
ca
Nal.7ikont,
hysical an
. A.. tor 0f.
,
Komit9kii, T.O., Candidat or Tsa~&-Acal Sciences ltayakiy. 3.M.,
Candidate of PI-qalcal and Mathematical Sciences, falmoTskly, L.K.,
Candidate of Physical and Mathematical Sciences, Killjanchuk, V.S..
C&Midat* of PhIslaal and Mathematical Sciences and Olauberiman.
h
olanaes.
A. Ye., Candidate of Physical and Mathematical
Cam 1/30
L!
Rzkov, A.V. Dependence of the Line Width In Ptanan
Spectrum on the Aggregate State of the Sub-
stance 229
Ress,"vv N.I. Photoelectric Study of th* Form end
Width of Piman Unes In Liquids and Solids 230
Favlovskaya, T. Ye., and,4A.-Pa"nakly. Variation
In Absorption spectra or Protein S61utlons Due to
Ionizing Radiation In Air and In Vacuum 235
LovAhlz, L.V., and A.P. Khavanskly. Spectroscopic
Study of the IonIzation of Molecules of AcrId1=
Compounds 240
K.711., I.V., and A.V. Shablys. Intrared-spootro-
&r.1"d. Study of the sensitization or the Photo.
oxidation of Organic Compounds by ftans of
AnthraquLnons Derivatives 243

VOLKOVA. M.S.; TONGUR. A.M.; CHUHAY,&VA. A.B.; ~~YTS~!! -- A.G.
Radiation determination of the molecular weight of Insulin [with
summ ry in Anglish]. Biofizike 2 no.4:465-468 '57. (ML13A 10:9)
1. Institut btokhimit im. A.M.Bakha Akademil nBuk SSSR. Moskva
(INSULIN) (MOLECULAR WMIGHTS)
(RADIATION-PHYSIOLOGICAL 17]r*CT)

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Theory of the biological effect of radiation (with summary In
English]. Biofizike 2 no-5:566-572 157. (MIRA 10:11)
1. Institut biokhimii Im. A.N.Bakha AN SSSR. Moskva.
(RADIATION--PHYSIOIDGICAI EFFECT)

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