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- W2002460449 abstract "1. A Suc-APA-MCA hydrolytic activity was significantly decreased in murine erythroleukemia cells during DMSO-induced differentiation, but not in DMSO-resistant cells. 2. The Suc-APA-MCA hydrolytic enzyme was purified by ion exchange, adsorption, gel filtration and affinity chromatographies. The results of the chromatographies showed that only one enzyme hydrolyzed Suc-APA-MCA in MEL cells. 3. This enzyme is more sensitive to hydrolysis by Suc-GPLGP-MCA than Suc-APA-MCA at slightly acidic pH, and its activity is stimulated by 2-mercaptoethanol. 4. A cysteine proteinase inhibitor did not affect the activity, but a specific inhibitor of prolyl endopeptidase, Z-thioprothiazolidine, completely inhibited it. These results suggest that the Suc-APA-MCA hydrolytic enzyme is identical to a prolyl endopeptidase." @default.
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- W2002460449 date "1991-01-01" @default.
- W2002460449 modified "2023-09-27" @default.
- W2002460449 title "Identification of an elastase-like activity, that decreased during the differentiation of mel cells, as a prolyl endopeptidase" @default.
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- W2002460449 doi "https://doi.org/10.1016/0020-711x(91)90012-c" @default.
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