Inactivation of cathepsin D by dithiophosgene and by 2,2-dichloro-1,3-dithiacyclobutanone

Autor: Emmanuel T. Rakitzis, T B Malliopoulou
Rok vydání: 1976
Předmět:
Zdroj: Biochemical Journal. 153:737-739
ISSN: 0264-6021
DOI: 10.1042/bj1530737
Popis: 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 μM;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.
Databáze: OpenAIRE