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Conversion of proinsulin to insulin: involvement of a 31,500 molecular weight thiol protease.

A lysed crude secretory granule fraction from rat islets of Langerhans was shown to process endogenous proinsulin to insulin with a pH optimum of 5.0--6.0. The converting activity in the lysed fraction was not inhibited by serine protease inhibitors (diisopropyl fluorophosphate, soybean trypsin inhi...

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Bibliografski detalji
Glavni autori: Docherty, K, Carroll, R J, Steiner, D F
Format: Artigo
Jezik:Inglês
Izdano: 1982
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC346725/
https://ncbi.nlm.nih.gov/pubmed/6750605
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