Biopolym. Cell. 1990; 6(5):59-64.
Structure and Function of Biopolymers
Molecular organization of human serum albumin structure
1Ostolovsky E. M., 1Botsyansky A. D., 1Borisenko S. N., 1Tolkachova N. V.
  1. M. V. Frunze Simferopol State University,
    Simferopol, USSR

Abstract

Physicochemical methods (IR- and NMR-spectroscopy, circular dichroism, etc.) that human serum albumin molecule is a compact globule with 50 % spiral structure and with exposition of a half of tyrozil on its surface. At the same time considerable percent of polypeptide chain with disordely packed form and with small contribution of β-structure part is observed in the molecule space structure. Theoretical calculations of α-spiral parts localization in serum albumin molecule indicate that approximately equal number of amino acids residues is found in every of three domains.

References

[1] Behrens P. Q, Spiekerman A. M., Brown J. R. Structure of human serum albumin. Fed Proc. 1975;. 34(5):591.
[2] Meloun B, Morávek L, Kostka V. Complete amino acid sequence of human serum albumin. FEBS Lett. 1975;58(1):134-7.
[3] Geisow MJ, Beaven GH. Large fragments of human serum albumin. Biochem J. 1977;161(3):619-25.
[4] Brown J. R. Structure of serum albumin: disulfide ridges. Fed. Proc. 1974; 38(4):33.
[5] Dugaiczyk A, Law SW, Dennison OE. Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982;79(1):71-5.
[6] Brown J. R. Structural originals of mammalian albumin. Fed Proc. 1979; 35(10):2141-4.
[7] Tiktopulo EI, Privalov PL, Borisenko SN, TroitskiÄ­ GV. Microcalorimetric study of the domain organization of serum albumin. Mol Biol (Mosk). 1985;19(4):1072-8.
[8] Mepherson A. Crystallization of proteins from polyethylene glycol. J Biol Chem. 1976; 252(9):6300-3.
[9] AzhitskiÄ­ GIu, Bagdasar'ian SN. Possibility of isolation of monomeric immunochemically pure serum albumin. Lab Delo. 1975;(12):712-4.
[10] OstolovskiÄ­ EM, ZadorozhnyÄ­ BA, Bocharov LP. Hydrophobic structure of blood serum and liver albumin in rabbits of different ages. Zh Evol Biokhim Fiziol. 1982;18(5):522-6.
[11] Troitskiy GV. New settlement system for protein conformation with spectropolarimetric data. Bioenergetics and biological spectrophotometry. Moscow, Nauka, 1967; 260 p.
[12] Chen YH, Yang JT, Martinez HM. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry. 1972;11(22):4120-31.
[13] Demchenko AP, Zima VL. UV spectrophotometry and the structure of proteins. Kyiv, Naukova Dumka, 1981; 208 p.
[14] Zav'yalov VP, Troitskiy GV. Hypothetical conformation of immunoglobulin G. Mol Biol (Mosk). 1973; 6 (7) :833-40.
[15] Izmaylova VN, Rebinder PA. Structuring in protein systems. Moscow, Nauka, 1974; 329 p.
[16] Gabuda SP, Rzhavin AF. Nuclear magnetic resonance in crystallohydrates and hydrated proteins. Novosibirsk, Nauka1978; 135 p.
[17] OstolovskiÄ­ EM, Mishin EN, Shadrin EN. Change of hydration properties of serum albumin in ontogenesis. Biofizika. 1983;28(5):874-5.
[18] Gusev EV, Turoverov KK, Rozanov YuM. Apparatus for measuring the spectral and polarization characteristics of luminescence. Functional morphology, genetics and biochemistry of cells. Leningrad, Nauka, 1974; 364-70.
[19] Vladimirov YuA, Dobretsov GE. Fluorescent Probes in the study of biological membranes. Moscow, Nauka, 1980; 320 p.
[20] Chirgadze YuN. Infrared spectroscopy of polypeptides and proteins. Itogi nauki i tekhniki. Moscow, VINITI, (Ser. Molekulyar. biologiya; Vol. 1). 1973; 9-61.
[21] Susie G. IR spectra of biological macromolecules and model compounds. Moscow, Mir, 1973; 345 p.
[22] Bellamy LJ. The infra-red spectra of complex molecules. London : Methuen New York : Wiley, 1958.
[23] Ostolovskiy EM, Afanas'yev SM, Zadorozhnyy BA. Infrared spectra of some mammalian serum albumin. Natural complexes of the Crimea, their optimization and security. Simferopol, 1984; 91-5.
[24] Eliot A. Infrared spectra of complex molecules. Moscow, Izd-vo inostr. lit., 1963; 382 p.
[25] Troitskiy GV. Electrophoresis of proteins. Kharkiv, Izd-vo Khar'k. univ, 1962; 323 p.
[26] Efimenko AM, Tolkacheva NV, Ostolovskii EM, Stanevich AV. Blood serum proteins during sport training. Ukr Biokhim Zh. 1978;50(6):723-6.
[27] TroitskiÄ­ GV, Kiriukhin IF, Tolkacheva NV, AzhitskiÄ­ GIu. The heterogeneity of electrophoretic albumin fractions under pathologic conditions. Vopr Med Khim. 1974;20(1):24-31.
[28] Tolkacheva NV, Bagdasar'ian SN, Efimenko AM, TroitskiÄ­ GV. Peculiarities of blood serum albumin transport function during physical exercise. Ukr Biokhim Zh. 1981;53(4):26-9.
[29] TroitskiÄ­ GV, Bagdasar'ian SN. Study of serum albumin denaturation. Biofizika. 1979;24(5):821-5.
[30] Aksenov SI, Kharchuk OA. On the state of water in solutions of proteins and viruses. Bound water in disperse systems. Moscow, University Press, 1977; Is. 4:118-38.
[31] Ostolovskiy EM, Mishin EN, Shcherbakov VN. Specific features of the conformational structure of serum albumin by NMR and IR spectroscopy. Tez. of reports I All-Union Biophys. Congr. Moscow, 1982; Ch. 1:87-8.
[32] OstolovskiÄ­ EM, BotsianskiÄ­ AD, ZadorozhnyÄ­ BA. Study of the structure of mammalian serum albumin using fluorescent probes. Biofizika. 1988;33(2):356-8.