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The fatty-acid-induced conformational states of human serum albumin investigated by means of multiple co-binding of protons and oleic acid.

作者信息

Dröge J H, Janssen L H, Wilting J

机构信息

Department of Pharmaceutical Chemistry, Faculty of Pharmacy, State University of Utrecht, The Netherlands.

出版信息

Biochem J. 1988 Mar 1;250(2):443-6. doi: 10.1042/bj2500443.

Abstract

The binding of oleic acid to human serum albumin causes progressive changes in (a) the pK of some amino acid residues, as detected by pH-stat titration and (b) the induced molar ellipticities of albumin-bound drugs (diazepam and oxyphenbutazone), as measured by c.d. It is concluded that albumin undergoes several conformational transitions as the amount of oleic acid bound increases from 0 to about 9 molecules/molecule of protein. At least three different conformations of the protein seem to be involved. These conformations can be linked with the three classes of oleic acid-binding sites on albumin.

摘要

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本文引用的文献

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