通过质子和油酸的多重共结合研究脂肪酸诱导的人血清白蛋白构象状态。
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
油酸与人类血清白蛋白的结合会导致以下方面的渐进性变化
（a）通过pH滴定法检测发现，一些氨基酸残基的pK值发生变化；（b）通过圆二色性测量发现，与白蛋白结合的药物（地西泮和羟苯丁酮）的诱导摩尔椭圆率发生变化。得出的结论是，随着结合的油酸量从0增加到约每分子蛋白质9个分子，白蛋白会经历几种构象转变。蛋白质似乎至少涉及三种不同的构象。这些构象可能与白蛋白上的三类油酸结合位点有关。
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