H-1-NMR OF ALBUMIN IN HUMAN BLOOD-PLASMA - DRUG-BINDING AND REDOX REACTIONS AT CYS(34)

被引：84

作者：

CHRISTODOULOU, J ^{[1
]}

SADLER, PJ ^{[1
]}

TUCKER, A ^{[1
]}

机构：

[1] UNIV LONDON,BIRKBECK COLL,DEPT CHEM,LONDON WC1H 0PP,ENGLAND

来源：

FEBS LETTERS | 1995年 / 376卷 / 1-2期

基金：

英国生物技术与生命科学研究理事会;

关键词：

BLOOD PLASMA; ALBUMIN; H-1; NMR; GOLD DRUG; DISULFIDE; THIOL;

D O I：

10.1016/0014-5793(95)01231-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

H-1 NMR methods are described which allow direct studies of the Cys(34) binding site of albumin in intact human blood plasma in vitro, Antiarthritic gold drugs and the alcohol-aversive drug disulfiram induce a structural transition detectable via H epsilon 1 and H delta 2 resonances of His(3) of albumin, and reactions of cystine, glutathione and captopril in plasma have also been investigated, Contrary to most assumptions, little of the albumin in normal plasma appears to be blocked at Cys(34) as a cystine disulfide.

引用

页码：1 / 5

页数：5

共 33 条

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