CALCULATION OF THE EFFECTIVE MACROMOLECULAR RADII OF HUMAN SERUM ALBUMIN FROM THE SHEAR VISCOSITY DATA FOR ITS AQUEOUS SOLUTIONS

被引:6
作者
Khorolskyi, O., V [1 ]
机构
[1] Poltava VG Korolenko Natl Pedag Univ, 2 Ostrogradskyi Str, UA-36000 Poltava, Ukraine
来源
UKRAINIAN JOURNAL OF PHYSICS | 2019年 / 64卷 / 04期
关键词
human serum albumin; aqueous solution; effective macromolecular radius; Malomuzh-Orlov theory; CONFORMATION; WATER;
D O I
10.15407/ujpe64.4.287
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
The Malomuzh-Orlov theory is used to analyze the experimental shear viscosity data obtained for aqueous solutions of human serum albumin (HSA) at pH = 7.0 in wide temperature and concentration intervals, which allowed the effective radii of HSA macromolecules to be calculated. It is shown that three intervals of the effective molecular radius of HSA with different behaviors can be distinguished in a temperature interval of 278-318 K: 1) below the crossover concentration, the effective molecular radius of HSA remains constant; 2) in the interval from the crossover concentration to about 10 wt%, the effective molecular radius of HSA in the aqueous solution nonlinearly decreases; and 3) at concentrations of 10.2-23.8 wt%, the effective radius of HSA macromolecules linearly decreases, as the concentration grows. The assumption is made that the properties of water molecules in the solution bulk play a crucial role in the dynamics of HSA macromolecules at the vital concentrations of HSA in the solutions. The role of water near the surface of HSA macromolecules and the corresponding changes of its physical properties have been discussed.
引用
收藏
页码:287 / 292
页数:6
相关论文
共 23 条
  • [1] Analysis of human serum albumin variants by mass spectrometric procedures
    Amoresano, A
    Andolfo, A
    Siciliano, RA
    Cozzolino, R
    Minchiotti, L
    Galliano, M
    Pucci, P
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1998, 1384 (01): : 79 - 92
  • [2] Bulavin L.A, 2010, FIZ ZHIVOGO, V18, P16
  • [3] Bulavin LA, 2006, J Struct Chem, V4, pS50, DOI [10.1007/s10947-006-0377-6, DOI 10.1007/S10947-006-0377-6]
  • [4] The conformation of serum albumin in solution:: A combined phosphorescence depolarization-hydrodynamic modeling study
    Ferrer, ML
    Duchowicz, R
    Carrasco, B
    de la Torre, JG
    Acuña, AU
    [J]. BIOPHYSICAL JOURNAL, 2001, 80 (05) : 2422 - 2430
  • [5] To What Extent Is Water Responsible for the Maintenance of the Life for Warm-Blooded Organisms?
    Fisenko, Anatoliy I.
    Malomuzh, Nikolay P.
    [J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2009, 10 (05) : 2383 - 2411
  • [6] ATOMIC-STRUCTURE AND CHEMISTRY OF HUMAN SERUM-ALBUMIN
    HE, XM
    CARTER, DC
    [J]. NATURE, 1992, 358 (6383) : 209 - 215
  • [7] Spectroscopic studies on human serum albumin and methemalbumin: optical, steady-state, and picosecond time-resolved fluorescence studies, and kinetics of substrate oxidation by methemalbumin
    Kamal, JKA
    Behere, DV
    [J]. JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2002, 7 (03): : 273 - 283
  • [8] Khmelevskii Yu. V., 1987, MAIN BIOCH CONSTANTS
  • [9] EFFECTIVE RADII OF MACROMOLECULES IN DILUTE POLYVINYL ALCOHOL SOLUTIONS
    Khorolskyi, O. V.
    [J]. UKRAINIAN JOURNAL OF PHYSICS, 2018, 63 (02): : 144 - 149
  • [10] Khorolskyi O. V., 2015, UKR FIZ ZH, V60, P882