Nonspecific reaction of a thiol: protein disulfide oxidoreductase with the disulfide bonds of insulin.
A thiol: protein disulfide oxidoreductase from bovine liver was isolated after separation from protein disulfide isomerase. The enzyme, after activation (reduction) with glutathione, was reacted with stoichiometric amounts of insulin and the sulfhydryl groups of the partially reduced hormone were labeled with iodo (l-14C)acetamide. After separation of the insulin chains, the radioactivity was found in both the peptides, with a ratio A-chain/B-chain equal to 2/1.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007328:Insulin / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008970:Molecular Weight; D010088:Oxidoreductases / Q000378:metabolism*; D011490:Protein Disulfide Reductase (Glutathione) / Q000378:metabolism*
D000596:Amino Acids; D004220:Disulfides; D007328:Insulin; D010088:Oxidoreductases; D011490:Protein Disulfide Reductase (Glutathione)