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1 H NMR of albumin in human blood plasma: drug binding and redox reactions at Cys 34
Author(s) -
Christodoulou John,
Sadler Peter J.,
Tucker Alan
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01231-2
Subject(s) - chemistry , cystine , albumin , glutathione , human serum albumin , redox , serum albumin , blood plasma , blood proteins , plasma protein binding , stereochemistry , cysteine , biochemistry , enzyme , organic chemistry
1 H 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 Hϵ1 and Hδ2 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.