Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases.
FEBS Lett
; 360(2): 101-5, 1995 Feb 27.
Article
em En
| MEDLINE
| ID: mdl-7875311
ABSTRACT
For the first time, three different stefins, A, B and C, have been isolated from a single species. The complete amino acid sequence of bovine stefin A was determined. The inhibitor, with a calculated M(r) of 11,123, consists of 98 amino acid residues. Although it exhibits considerable similarity to human and rat stefin A, some significant differences in inhibition kinetics were found. Bovine stefin A bound tightly and rapidly to cathepsin L (kass = 9.6 x 10(6) M-1.s-1, Ki = 29 pM). The binding to cathepsin H was also rapid (kass = 2.1 x 10(6) M-1.s-1), but weaker (Ki = 0.4 nM) due to a higher dissociation rate constant. In contrast, the binding to cathepsin B was much slower (kass = 1.4 x 10(5) M-1.s-1), but still tight (Ki = 1.9 nM).
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cistatinas
/
Inibidores de Cisteína Proteinase
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Eslovênia