1H NMR of albumin in human blood plasma: drug binding and redox reactions at Cys34.
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 H epsilon 1 and H delta 2 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.
Christodoulou
J
J
Department of Chemistry, Birkbeck College, University of London, UK.
Sadler
P J
PJ
Tucker
A
A
D000427:Alcohol Deterrents / Q000378:metabolism / Q000494:pharmacology; D000959:Antihypertensive Agents / Q000378:metabolism / Q000494:pharmacology; D018501:Antirheumatic Agents / Q000378:metabolism / Q000494:pharmacology; D001310:Auranofin / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites / Q000235:genetics; D001798:Blood Proteins / Q000378:metabolism; D002216:Captopril / Q000378:metabolism / Q000494:pharmacology; D003545:Cysteine / Q000378:metabolism*; D004220:Disulfides / Q000378:metabolism; D004221:Disulfiram / Q000378:metabolism / Q000494:pharmacology; D006052:Gold Sodium Thiomalate / Q000378:metabolism; D006639:Histidine / Q000378:metabolism; D006801:Humans; D007526:Isoelectric Point; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D015394:Molecular Structure; D010084:Oxidation-Reduction; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*
D000427:Alcohol Deterrents; D000959:Antihypertensive Agents; D018501:Antirheumatic Agents; D001798:Blood Proteins; D004220:Disulfides; D012709:Serum Albumin; D006052:Gold Sodium Thiomalate; D001310:Auranofin; D006639:Histidine; D002216:Captopril; D003545:Cysteine; D004221:Disulfiram