Chymotrypsinogen: an activating enzyme in the mitochondrial membrane of rat submaxillary gland.
Biochem Int
; 25(6): 1035-41, 1991 Dec.
Article
em En
| MEDLINE
| ID: mdl-1725694
ABSTRACT
A peripheral membrane protease was purified from mitochondria of rat submaxillary gland. On non-denaturing PAGE the purified enzyme showed a single protein band with the enzyme activity. It yielded two protein bands with molecular weights of 39 KDa and 20 KDa on SDS-PAGE, indicating that the enzyme is composed of two protein components. The enzyme activity was strongly inhibited by SBTI, aprotinin and benzamidine. PMSF, TLCK and EDTA did not produce inhibition. The enzyme could hydrolyze different synthetic substrates having arginine at the P1 position with highest affinity for the substrate Bz-Phe-Val-Arg-p-nitroanilide was noted. The enzyme showed significant activation of chymotrypsinogen A.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Glândula Submandibular
/
Quimotripsinogênio
/
Mitocôndrias
Limite:
Animals
Idioma:
En
Revista:
Biochem Int
Ano de publicação:
1991
Tipo de documento:
Article