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Regulation of hormonal and secretory granule membrane di sulfides by adeno hypophyseal glutathione di sulfide oxido reductase


, : Regulation of hormonal and secretory granule membrane di sulfides by adeno hypophyseal glutathione di sulfide oxido reductase. Life Sciences 28(20): 2309-2316

An NADPH-dependent glutathione:disulfide oxidoreductase (thioltransferase) was identified in and partially purified (12.3-fold) from porcine adenohypophyseal cytosol. The enzyme is specific for NADPH and reduced glutathione, but the disulfide substrates include a wide size range (glutathione, cystine, RNase, oxytocin, vasopressin, monomeric and oligomeric growth hormone and prolactin). It also utilizes secretory granule membrane proteins. Substrate specificity studies (including utilization of cystine and failure to utilize insulin) and physicochemical properties (MW 180,000) distinguish this enzyme from other glutathione:disulfide oxidoreductases. This thioltransferase may play a regulatory role in the hormone secretory process by control of the thio:disulfide oxidation state of disulfide-bonded oligomers or of granule membrane proteins.

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Accession: 006288492

PMID: 7253822

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Related references

Lorenson, M.Y.; Lee, Y.C.; Jacobs, L.S., 1981: Regulation o hormonal and secretory granule membrane disulfides by adenohypophysial glutathione: disulfide oxidoreductase. An NADPH-dependent glutathione:disulfide oxidoreductase (thioltransferase) was identified in and partially purified (12.3-fold) from porcine adenohypophyseal cytosol. The enzyme is specific for NADPH and reduced glutathione, but the disulfide subs...

Anonymous, 1974: Coenzyme a glutathione reductase ec 1646 and glutathione reductase ec 1642 from rat liver 2 di sulfide oxido reductase activities in 1 protein entity

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