| Literature DB >> 942386 |
E T Rakitzis, T B Malliopoulou.
Abstract
Cathepsin D, purified from bovine spleen, is inactivated by the unstable inhibitors dithiophosgene and 2,2-dichloro-1,3-dithiacyclobutanone. Inhibition constants are identical for both of the compounds tested: Ki 96.1 muM;k/c0.406. It appears that the active species is 2,2-dichloro-1,3-dithiacyclobutanone, to which dithiophosgene is hydrolysed before cathepsin D inactivation.Entities:
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Year: 1976 PMID： 942386 PMCID： PMC1172645 DOI： 10.1042/bj1530737
Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857