CONFORMATIONAL-CHANGES IN HUMAN-SERUM ALBUMIN AROUND THE NEUTRAL PH FROM CIRCULAR DICHROIC MEASUREMENTS

被引：90

作者：

WILTING, J ^{[1
]}

WEIDEMAN, MM ^{[1
]}

ROOMER, ACJ ^{[1
]}

PERRIN, JH ^{[1
]}

机构：

[1] UNIV FLORIDA,J HILLIS MILLER HLTH CTR,COLL PHARM,GAINESVILLE,FL 32610

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 579卷 / 02期

关键词：

Albumin; Circular dichroism; Conformation; N-B transition; Serum albumin; Warfarin-albumin;

D O I：

10.1016/0005-2795(79)90075-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The molar ellipticity of the warfarin-albumin complex at 310 nm increases with pH from 6 to 9. This pH dependence runs parallel with that of the molar ellipticity of the albumin alone at 292 nm. The change in molar ellipticity with pH occurs in a smaller pH interval after addition of the physiological concentration of calcium ions. These findings give support to the assumption that the binding site for warfarin on the albumin molecule is affected by the neutral-to-base transition in the protein. © 1979.

引用

页码：469 / 473

页数：5

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