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

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, Antia rthritic gold drugs and the alcohol-aversive drug disulfiram induce a structural transition detectable via H epsilon 1 and H delta 2 resonan ces of His(3) of albumin, and reactions of cystine, glutathione and ca ptopril in plasma have also been investigated, Contrary to most assump tions, little of the albumin in normal plasma appears to be blocked at Cys(34) as a cystine disulfide.