SCIENTIFIC ABSTRACT G.A. DEBORIN - I. DEBRECZENI

• Document Type: CREST
• Collection: Scientific Abstracts
• Document Number (FOIA) /ESDN (CREST): CIA-RDP86-00513R000309910013-5
• Release Decision: RIF
• Original Classification: S
• Document Page Count: 100
• Document Creation Date: November 2, 2016
• Document Release Date: June 12, 2000
• Sequence Number: 13
• Publication Date: December 31, 1967
• Content Type: SCIENTIFIC ABSTRACT

SOV/20-121-1-39/55
The Molecular Vieizht of Serum Albumin, Exposed to Ultra-Sonic i;aves in the
U
Presence of Different Gases
The latter do not lose the capacity of forming a monomolecular
layer. A fission of the protein molecules was observed also in
the case of an acoustic irradiation of serum albumin solutions
of higher concentration (Table 2). There J_s no interaction
between the splinters of the protein molecule, they are sitable,
if the acoustic irradiation takes place in the presence of oxy.-
gen (Table 3). The above mentioned investigation makes possible
the investigation of the correlation between structure and
function of the protein bodies. There are 1 figure, 3 tables,
and 9 references, 7 of which are Soviet.
ASSOCIATION: Institut biofiziki Akademii nauk SSSH (Institute of Biophysics,
AS USSR) Institut biokhimii im. A. N. Bakha Akademii nauk SSSR
(Institute of Biochemistry imeni A. 11. Bakh,AS USSR)
PRESENTEDt March 10, 1958, by A. I. Oparin, Member, Acade::.y of Sciences,
USSR
Card 3/4

AUTHORS: Deborin, G. A., Ivashchenko, G. W., SGIV/20-122-4-31/57
B y s rr-o Tt-,
TITLE: An Investigation of Egg Albumin and Carotene Complexes
(Issledbvaniye kompleksov yaic:hnogo al'bumina s karotinom)
PERIODICAL: Doklady Akademii nauk SSSR, 1958, Vol 122, Nr 4, pp 650-1652
(USSR)
ABSTRACT: It is known that the lipoprotElins of the blood serum contain,
in addition to sterols, a considerable amount of carotenoides
also (Ref 1). Carotene, however', is not in colloidal solution
in the blood serum, as contrasted with previous conceptions,
but is closely combined with the albumins of the blood (Ref 2).
In reference 3 it was proved by electrophoresis that carotene
possesses a specific affilhity to the serum globulin. The
carotene containing lipoproteins fo~rm widespread and often
physiologically important pigments in the organism. According
to a survey of publicattons (Refs 4-8) the authors denote the
purpose of the present paper as the investigation of the
interactions of carotene with egg albumin under the conditions
Card 1/4 described in their previous papers dealin.- with sterols (Ref 7).

'7
An Investigation of Egg Albumin and SOV/20-1 210-4-13 1./51
Carotene Complexes
The ultraviolet absorption spectra were measured by the
spectropliotometerff.411 -4 withinthe wave range between
240 and 300 me - It was first proved that the variation of the
absorption intensity is not due to a denaturation of the
albumin but to the complex foimation. Figure 1 shows typical
absorption curves of the egg a1bumin (Curve 1) and of the
complex of the egg albumin with carotene (Curve 2) in the
quoted range (ordinante - extinction, abscissa - wave lengths).
From this it is seen that in the formation of the mentioned
complex the absorption maximum of the albumin at 280 me is not
altered, but a distinct variation of the absorption intensity
takes place. It was proved (Ref9) that such a variation is
caused by various factors, among others by the variation of the
state of aggregation of tho protein molecules, even if they
remain chemically unchanged. This means that the chromophore
groups are not involved in such a process. The reduction of the
absorption maximum by protein solutions in the complex formation
with carotene is due to a comt-ination of aggregation- and
denaturation effects and cannot be taken as a quantitative
measure of the complex formation. Nevertheless, this method
Card 2/4 has proved suitable for the qualitative identification of the

An Investigation of Egg Albumin and SOV/20-122-4-51/57
Carotene Complexes
nascent protein-carotene complex. Parallel spectral
investigations on monomoleoular layers supported this
conclusion. Figure 2 shows isotherms of the compressibility
of a monolayer of egg albixnin (curve 1) and of the
egg albumin-carotene complex in a 5 'p'f solution of ammonium
sulfate. From the above experimental results the conclusion
may be drawn that at 40 0 the egg albumin forms a complex
which is stable in a broad pH-range. By this neans carotene
is protected by the protein against oxidation by atmospheric
oxygen. There are 2 figures, 1 table, and 11 references,
9 of which are Soviet.
ASSOCIATION: Institut biokhimii im. A. N. Bakha Akademil nauk SSSR
(Institute of Biochemistry imeni A. N. Bakh of the Academy
of Sciences,USSR)
PRESENTED: April 23, 1958, by A. I. Oparin, Academician
SUBMITTED: April 22, 1958
Card 3/4

OPARIN, Aleksandr Ivanovioh, Andemik; G,~., knni[Ahim.nauk,
red.; ICAM, Ya.M., red. izd-ve-,-______ -U, R.P.. tekhn.red.
(Origin of life] Proiekhozhdenie shisni. Moskva, Voon.izd-vo
H-va oborony SM, 1959- 125 P. (MIRA 12:10)
(Life--Origin)

HLIPINER. I.Ye.; DKBORIN, G.A.; ZORINA, O.M.
Molecular weight andEctivity of proteolytic enzymes irradiated with
ultrasonic wavos. Biokhimiiia 24 no-5i8l7-822 S-0 159. (MIRA 13:2)
1. Institut biologicheskoy fiziki i Inotitut biokhimii im. A.N.
19akha. Akademii nauk SSSR, Moskva.
(PROTFLASES chem. )
(ULTRASONICS eff.)

111301aff, G.A.
Fifth International Congress of Biochemistry. Biokhimiia 24 no-5S
954-955 S-0 '59. (BIOCHEMISM-CONGUSSFIS) (MIRA 13:2)

170) V/20-124-3-5--1/67
AUTHORS% Deborin, G. A., Bystrova, hl. I., Ivanova, V. F.
TITLE: Changes in the Proteolysis Process of Serum Albumin Caused by
Tripsin in the Formation of Complexes of the Ferment or of the
Substrate With EBtradiol (Izmeneniye khoda proteoliza syvorotoch-
nogo al'bumina tripsinom pri obrazovanii komuleksov fermenta ili
substrata s eatradiolom)
PERIODICAL. Doklady Akademii nauk SSSR, 1959, Vol 124, Nr 3, pp 665-68i (USSR)
ABSTRACT: On a previous occasion (Refs 1-3), the authors had proved that the
unstable complexes of certain proteins are more stable to various
influences than are the initial. proteins. Eatradiol, too, is one
of the water-insoluble sterols that can combine with senui albumin
outside the ozanism (average: 0.43 mol estradiol per 1 molecule
protein)(Ref 4 . For this reason, the authors investigated the
estradiol linkage to proteins under the same conditions ,Lnder which
the linkage with ergosterol took place. An investigation was made
into the changes which cause the complex formation of the ferment
or of the substrate with eatradiol in the proteolysis of serum
albumin. It was found that, analogous to ergosterol, estradiolforms
unstable complexes with proteins which participate in the proteo-
Card 1/3 lytic process, Thus the proteolytic process is slowed down, and the

S011/2U- 124-3-515/67
1
Changes in the Proteolysis Piozess of Serun Aibum:~n Caused by 7.ripsin in the
Formation of Complexes of the Perment or of the Substrate With Estradiol
splitting intensity of the substrate by the ferment is reduced.
This result can be naturally explained by 'the fact that the com-
plex formation stabilizes the Froteilyl agai-n-st influences which
disturb the protein atructure~ In the formation of the complex
of a proteolytic, ferment with sterol, the activity of the ferment
in the complex is higher than fhe activity cif the initial ferment.
In the opinion of the authors, this phenomenon can be explained
by the fact that, as a sonsequonse of tha zomplex formation, the
ferment is More reSiStglLt to the disactivati.on resulting from its
denaturat-i3n and autodi&estion., These data confirm the view that
the-complex formation of prote:'Ins with lipoids constitutes one of
the factors that contr.---! the enzymatic processes within the cell.-
There are 4 figures and 6 refe:rences, 4 of which are Soviet.
ASSOCIATION: Institut biokhitaii im. A. N. Bakhu Akademii nauk SSSR
(Institute of Biochemistry iaieni A. 1I. Bakh of the Academy of
Sciences, USSR)
Card 22/3

DE30RIN. G.A.
Der zweite Weltkrieg; llilitaroplitacDer Abriss.
Berlin, Verlag des Ainisteriums fur ationale Verteiddung, 1960.
1488 p. tables.
Trz;nslated from the original Russian title; Vtoraya hirovaya Voynii.

pjMggjN,G.A-; IVANOVA,V.P... OPARIN,A.I.; ILODI,P.
Zffect of ergosterol on the enzymatic activify of ;ihosphoglyceraldehyde
dehydrogenase. Acta phyetol.hung 17 no.2:133-140 160.
1. Inetitut biokhtmit A9N. 633R. la Balcha, Moskva, I Institut
biokhimil A.N.- Vengrli, Budapeaht.
(DXMROQMUMS wtab,)
(UTAMIN D Oharmacol)

T)VTJ rR T 1-3
Z., 1"A111OVA, V. P., -ind 7:-~K711TYOVA, A.
r
(U-SS-R
"The Controlling Effect of the Combination of Proteins with Sterols
nnd Nucleic A7id and of Ad!iorption Phenomena in the Course of some
Enzymic Processes (read by title).
Report presented at the 5th International Biochemistry Congress,
Moscow, 10-16 Aug 1961

MKRTUMOVAP N.A.; DEBORIN G A
Enzymatic activity of ribonucleaBe adsorbed on EBS-I+ sulforesin.
Dokl, AN SSSR 146 no.6:1434,3436 0 '(2. (141RA 15:10)
1- Institut biokhimii im. A.N. Bakha AN SSSR. Predstavleno
akademikom A.I. Oparinym.
(RIBONITCLEASE) (ION EXCHANGE RESINS)

GURVICII, A.Ye.; ENGELIGARDT, V.A., akademik, glav. red.; DEBMIRl"
G.A., zwp.. glav. red.; UMBER, L.A., prof., rt~d.;
BUZNIKOV, G.A.,, red.
[Viroloa and .;m.unology; prchlems of gcneral vivology,
st.ru-cture an(I bjo~;ynthe,,,is of ant-lborileg]
1'~.nlunc'joi-rlln; ll-l'c*")Icn;y oi'~~'IvJlel struktura i
27i.
(MT.`~4 18:1)
1. Peystvitellnyy chier, AMN SSSIR (fcr ",'illber).

YAKOVLEV, V.A.; ETTGFLIGAiW, V.A., akademik, lylav. red.; DEBORIP,
G.A., zam. glav. red.; BRAUN'SlITEYN, IL.Ye., akaderik, red.
FOZNZSfUYA, A.A., red.
[Enzymes] Fermenty. Yoskva, Nauka, 3.964. 310 p.
(MIfU 17:9)

KRETOVICH, V.L.p otv. red.; PAVIOVSKAYA, T.Ye-0 kand. Wol.nauk,
red.; DEBORIN G A., kand. khl--,P,. naul-p xed.; YIUSILINIYOVA,
z r"M OVSHY, Yu.A., red.izd-va; AS7AF'Yh'VA,
G.V.p
G.A., tekhn. red.
(Problems of evolutionary and technical biochemistry; on
the 70th birthday of Acaeemician A.I.Oparin] ProbleuW evo-
liutsionnoi i tekhnIcheskoi blokhintli; k 70-letiiu akade-
mika A.I.Oparina. Moskva, Izd-vo 19iauka," 1964. 363 p.
(MIAA 170)
1. Akademiya nauk SSbTL. Institut biokbimii. 2. Chlen-
korrespondent AN &SM (for Kretovich).

SPYiOYLOV, V.I.; ENGELIGARDT, V.A.9 akademik, glav. red.; DEBORIP,
G*A.p zam. glav. red.; VASILIYEV, Yu.M,, prof.,, red.
(Biology of malignant growth] Biologiia. zlokachesivennogo
rosta. Moskvap Nauka, 1965. 254 p. (MIRA 18.6)
N

ODINTSOVA, M.S.; ENGELIGARDT, V.A., akademik', glav. red.;
DEBORIN, G.A., zam. glav. red.; SPIRIN, A.S., doktor
biol. nauk, red.
[Biosynthesis of protein and nucleic acids] Biosintez belka
i nukleinov-ykh kislot. Moskva, lqauka, 1965. 346 p.
(MIRA 18:4)

DEBORM, G.A.; BjjIUJ:OtTA, V.Z.; ZHUKOVA, I.G.
Study of phosphoDpide surface films of Micrococcun lysodeicticuo
membraneo tit the water-air interface.rukl. All SSSR 159 no.5:
1161-1164 D 164 ( MFRA 28t1)
1. Institut biokhiniii im. A.N. Dakha fiN SSSR. Pred.9ti-vleno fika-
damIkom A.T. Oparinym.

OPARIN, A.I.; DEBORIN, G.A.
Modeling an active transfer of protein through lipid membranes.
Ukr.biokhlm.zhur. 37 no.5.-761-766 165-
(MIRA 18:10)
1. Inatitut bickhimii im. A.N.Bakha AN SSSR, Moskva.

BARANOVA, T.Z.; '101KOVA, I.G.; DEBOR N, G. .
.1
IntArrelationship betwoun the phospholipids from the membralias
or Microooccus lysodaikticus and somm, albumiwi in tho monolayar
at the bourktary line watAr-a-ir. Dokl,, AN SSSR 165 nu.'Lt-431-434
N 165. (MIRA 18~1.11.)
1. IwO-Uull- bio'kh"zi1j, im. A.N. Ri0in AN SSSR. SOILI ~tvid Jaivwirv
14, 1S65.

DEBORIN G.A.; TYURINA, I.P.; TOFXHOVSUYA, T.I.; OPART-N, A.I.
--l' -
alzymatic splitting of ribanucleic acid separated ftom ribn.-
nuclease by a lipid membrane. Zhur. elrol. biokhim. i fi7-lol.
no. 6:550-556 N-D 1/05 WITU 19-1)
1. Thstitut biokhimii imeni A.N. Bakha AN SSSR, Moskim. Sub-
mitted May 24, 1965.

s c f

.-",! ! , .* , , 1 -1 ,
:". 1 A J. 1, .
Treatment of urolo-i-3al liseases at the iruskavets health resort. 3ov. :~.-ed.
1,~
I., I.o 11, 1952.

DEBORSKI, T.
"For a proper trend in the development of the food siuhstitutes Industry,"
Przemysl Rolny I Spozywczy, "-I:arszawa, 'Vol 8, Yo S, Aug. 1954, p. 287.
SO: Eastern European Accessions List, Vol 3, No 11, Yov 1954, L.C.

. . ......... .............. ... ....=
,MW/X*dIoIw - Albumen oo t 48
Medicine - Celle
"Albume-is of Cell Nuclei," 1. B. Zbarekiyl S. a.
Dabov, en Sot Res Oncol Inst imeni P. . Gertsen,
3 3/4 pp
'"Dok Ak Nauk SSSR" Vol LIUI, No 6
Obtained three albumen fractions bv various proev-
-I-ftee frorm cell nuc2ei: a nucleoprotaid, an acid
albumen, ani a residual al .bumen. Their most Im-
portant characteristic is their amino acid compo-
altion. The acid albumen corresponds to Stedm=
Ana Stedman's chromosonin. No detailed study has
0
UM/Medicine - Albumen (Contd) Oct 48
'been made of the residual albumen. Submitted b7
Aced A. I. Oparin 30 Aug 48.
60/49251

DXBOV, S.S.
---W------- MOW.
Opantitative content of protein fractions in call nuclei of normal
tiesut and in malignant tumors. Biokhtmiia, Moskva 15 no.61314-320
Nov-Doe 50. (CL4L 21:1)
I.Blochenical, Laboratory. Central Oncological Institute, Moscow.

Amount of promerla fractloats im tho coil nuchil at normal
and mal4past tissues. ;. S. I-elltre (Cvt,tr.1 (h ~hwmd
ItAkiworw Ift *3I4-'-NKI%l5l~j"lhv 11-11
I I'l nottlial All'I mallselaill 11.;~" W "tall "till OW111A.
',t.fllmst *1 plottrio fractittra. (1) nueleopful eh$ (CRI'l. by M
x4cl 1, (2) acidic Protein (Millue ext'l. by 0.05 N N201 11.
aud t3) re4lual pnArin. The iturleq,rottein coatent III
stottiml human liver cril mirlei vari" Irom 42 fit WO- acidic
I'mccio 35 51%. and f"'Ittal 1wolent 4 'A-I M' - -
, The uts
vleolmlt call of calivritals fillulall fivir rell ~11'-Trl
to dvidlv pf"Irm 1111", ated 1"HII'll pf"IeW W 11". 1 he
~llllv relalk"I i. "ItwTv"I Its ntlellIA arld 111411ralAut tat cell
Irlei. PrieAllry

ZBAR IY,I.B.; MBOV, S.S.
Protein fractions of call nuclei. Biokhimiya, 151. 16, )W-195.
(BA - A III Kr 153:267) (MIRA 4:10Y

DEBOV, S. S.
"The Quantitative Content of Protein Fractions in the Cell Nuclei of
Certain Benign Tumors of Einbryonic and Regeneratin!T Tissues", Vopr. Med.
Khimii, No. 6, Pp 117-124, 1953.
The amount of acidic proteins and nucleoproteids in Vie cell nuclei
of uterine fibromyomas, fetal tissues, liver se".tions from rats, and re-
generating tissues was investigated. The author sugc~ests that the increase
in the residual protein content of cell nuclei is connected with a process
of tissue dedifferentiation (or anaplasia in tumors), while an increase in
the quantity of nucleoproteids, on the other hand, is due to differentiation.
SO: Sum. No. 443, 5 Apr 55

DEBOV. S.S. (Moskva)
Nucleic acids under normal and pathologit, cond1tions. Usp.biol.khim.
2:115-140 154. (MIRA 12:12)
(NUCLZIC ACIDS. metabolism,
in Patbol. & normal cond,,

IEBOV, S., kandidat biologicheskikh nauk.
Proteins and protein metabolism in cancer (Raview of foreign
periodical literature). Soyr.probl.onk. 6 no-5:3-8 '54.(KLRA 7:7)
(Cancer) (Proteins)

USSR/Medicine Biochemistry
Card 1/1 Pub. 22 - 27/45
Authors : Debov, S. S.
Title : 460iyiation oi~'uracil in tissue homogenateis
Periodical : Dok. AN S5SR 99/4., 589-592., Dee 1, 1954
Abstract : The possibility of the formation of thymino in tissue homogenates, through
direct methylation (remethylation) of urac.11, was investigated. The results
are listed. Ten references: 6-TJSSft; 3-USA and I.-Finglish (1933-1953).
Drawings.
Institution : The First Medical Institute, Moscow
Presented by: Academician A. D. Speranskiy, June 2, 1954

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