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Binding of water and electrolytes to proteins. An equilibrium dialysis study
Author(s) -
Bull Henry B.,
Breese Keith
Publication year - 1976
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1976.360150811
Subject(s) - chemistry , hemoglobin , albumin , electrolyte , carbon monoxide , bovine serum albumin , serum albumin , salt (chemistry) , dialysis , chromatography , salting out , inorganic chemistry , saturation (graph theory) , biochemistry , organic chemistry , aqueous solution , medicine , electrode , catalysis , mathematics , combinatorics
The technique of equilibrium dialysis has been used to study water and salt binding to egg albumin, to human carbon monoxide hemoglobin, and to bovine serum albumin. The salts used were CsCl, KCl, NaCl, LiCl, Gu·HCl, NaBr, Cs 2 SO 4 , K 2 SO 4 , Na 2 SO 4 , Li 2 SO 4 , and Gu 2 SO 4 . The amount of water bound by proteins depends on the probe being used. Sulfates tend to bind to proteins and they also increase the water binding. At saturation, about 41 and 140 mol Gu·HCl bind to 1 mol egg albumin and to 1 mol carbon monoxide hemoglobin, respectively. Both proteins are dehydrated by Gu·HCl. The hydrodynamic hydration of egg albumin as determined by viscosity appers to increase as the relative viscosity of the medium increases.