H-1-NMR OF ALBUMIN IN HUMAN BLOOD-PLASMA - DRUG-BINDING AND REDOX REACTIONS AT CYS(34)
H-1-NMR OF ALBUMIN IN HUMAN BLOOD-PLASMA - DRUG-BINDING AND REDOX REACTIONS AT CYS(34)
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DOI：
10.1016/0014-5793(95)01231-2
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发表时间：
1995-11-27
期刊：
影响因子：
3.5
通讯作者：
TUCKER, A
中科院分区：
文献类型：
--
作者：
CHRISTODOULOU, J;SADLER, PJ;TUCKER, A
用H-1核磁共振方法可以在体外直接研究完整人血浆中白蛋白的Cys(34)结合部位，抗关节炎药物和酒精厌恶药物二磺拉姆诱导白蛋白His(3)的His(3)的H epsilon 1和H Delta 2共振可检测到的结构转变，也研究了血浆中胱氨酸、谷胱甘肽和卡托普利的反应，与大多数假设相反，正常血浆中的白蛋白似乎很少被Cys(34)阻断为半胱氨酸二硫化物。
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.