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- W1978769726 abstract "GSH-insulin transhydrogenase catalyzes the inactivation of insulin via sulfhydryl-disulfide interchange between the disulfide bonds of insulin and a thiol donor. In addition to simple thiols such as GSH, purified glutathione-insulin transhydrogenase has been found to be able to utilize the thiol groups of proteins as co-substrates for the degradation of insulin (measured by the solubilization of 125I-labeled insulin in trichloroacetic acid). Thiol proteins found to be effective co-substrates include alcohol dehydrogenase, hexokinase, fructose-1,6-diphosphatase, malate dehydrogenase, glyceraldehyde phosphate dehydrogenase, glycerol phosphate dehydrogenase, reduced insulin A and B chains, and reduced ribonuclease. Lactate dehydrogenase, aldolase, phosphorylase a, urease, glutathione reducatase, pancreatic lipase, S-sulfonated insulin A and B chains, and native ribonuclease show no activity as co-substrates. The low concentrations of thiol proteins necessary to show insulin degradation indicate the possibility that GSH-insulin transhydrogenase migth utilize protein thiols, in addition to glutathione, as physiologic co-substrates for insulin degradation." @default.
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- W1978769726 date "1973-09-01" @default.
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- W1978769726 title "Insulin degradation VIII. Protein thiols as co-substrates for glutathione- insulin transhydrogenase" @default.
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- W1978769726 doi "https://doi.org/10.1016/0304-4165(73)90306-1" @default.
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