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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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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1982
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC346725/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6750605/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.79.15.4613 |
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