Reaction of insulin with reduced glutathione.
An aggregate of insulin, molecular weight about 70,000, was formed when it was incubated with GSH. The aggregate product converted to a low molecular weight product, presumably the insulin A- and B-chains, on addition of urea to mixtures. This conversion requires sulfhydryl-disulfide interchange as a sulfhydryl reagent inhibited it, in part. The aggregate does not form with EDTA in mixtures, but as before, a product of lower molecular weight than insulin was formed. These results support the previously held view that the disulfide bonds formed by insulin are influenced by its structure.
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Department of Biochemistry, West Virginia University School of Medicine, Morgantown 26506.
D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D004492:Edetic Acid; D005978:Glutathione / Q000378:metabolism*; D007328:Insulin / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight
D007328:Insulin; D004492:Edetic Acid; D005978:Glutathione