Activation of choleragen by thiol: protein disulfide oxidoreductase.
作者： J. Moss , S.J. Stanley , J.E. Morin , J.E. Dixon
DOI: 10.1016/S0021-9258(19)70255-5
关键词: Oxidoreductase 、 Protein-disulfide reductase (glutathione) 、 Arginine 、 Peptide 、 Glutathione 、 Dithiothreitol 、 Protomer 、 Biochemistry 、 Thiol 、 Chemistry
摘要: Abstract In the presence of thiols such as glutathione or dithiothreitol, choleragen catalyzes NAD-dependent ADP-ribosylation arginine and proteins; reduce disulfide linking A1 A2 peptides A protomer toxin, releasing active peptide. Homogeneous thiol:protein oxidoreductase from bovine liver, in limiting concentrations increased rate activation its protomer. The ability preparations to activate co-chromatographed with protein on gel permeation columns was proportional concentration assay. oxidoreductase, dithiothreitol necessary for were reduced. Thiol:protein could play a role reduction release catalytically
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