Cathepsin S and cruzipain are inhibited by equistatin from Actinia equina.
Biol Chem
; 380(5): 589-92, 1999 May.
Article
en En
| MEDLINE
| ID: mdl-10384966
ABSTRACT
Cathepsin S has been isolated for the first time from human tissue. It has a molecular mass of 24 kDa and an isoelectric point in the range of 8.2 to 8.6. The enzyme is inhibited by equistatin, which belongs to the thyropins, a new family of protein inhibitors, with an inhibition constant of Ki = 0.40 +/- 0.07 nM. Cruzipain, a cathepsin L-like enzyme sharing a 130 amino acid long C-terminal extension, is also strongly inhibited by equistatin (Ki = 0.028 +/- 0.006 nM). Together with previously reported data, these results further indicate that a functional heterogeneity exists among thyropin inhibitors, as demonstrated by their interaction with cathepsin S and cruzipain.
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Colección:
01-internacional
Asunto principal:
Anémonas de Mar
/
Cisteína Endopeptidasas
/
Proteínas
/
Catepsinas
/
Inhibidores de Cisteína Proteinasa
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biol Chem
Asunto de la revista:
BIOQUIMICA
Año:
1999
Tipo del documento:
Article
País de afiliación:
Eslovenia