1H NMR of albumin in human blood plasma: drug binding and redox reactions at Cys34

FEBS Letters

Christodoulou, John¹  Sadler, Peter J.¹  Tucker, Alan¹ 

[1] Department of Chemistry, Birkbeck College, University of London, Gordon House, 29 Gordon Square, London WC1H 0PP, UK

关键词: Blood plasma;    Albumin;    1H NMR;    Gold drug;    Disulfide;    Thiol;   

DOI  :  10.1016/0014-5793(95)01231-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

¹H NMR methods are described which allow direct studies of the Cys³⁴ 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 Hϵ1 and Hδ2 resonances of His³ 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 Cys³⁴ as a cystine disulfide.

【 授权许可】

Unknown