Purification and properties of thiol protease inhibitor from rat liver cytosol.
Biochim Biophys Acta
; 669(1): 21-7, 1981 Jun 29.
Article
en En
| MEDLINE
| ID: mdl-7028126
ABSTRACT
Thiol protease inhibitors were found in the cytosol fractions of various rat tissues. An inhibitor, named cytosol thiol protease inhibitor, was purified from rat liver cytosol by acid treatment and column chromatographies on Sephadex G-50, DEAE-Sephadex and Sephadex G-75. The purified inhibitor gave a single protein band on sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The molecular weight of the inhibitor was found to be 12 400 by gel filtration on Sephadex G-75 and SDS-polyacrylamide gel electrophoresis, and its isoelectric point was found to be 5.04. This inhibitor inhibited rat liver lysosomal cathepsin B, B2, C, H and L and papain, but not cathepsin A or D, trypsin or chymotrypsin. The inhibitor caused noncompetitive inhibition of the hydrolytic activity of cathepsin H on alpha-N-benzoyl-DL-arginine 2-naphthylamide and its Ki value was 4.08 . 10(-8) M. Heat treatment at 80 degrees C for 10 min reduced the activity 40%.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Inhibidores de Proteasas
/
Hígado
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1981
Tipo del documento:
Article
Pais de publicación:
HOLANDA
/
HOLLAND
/
NETHERLANDS
/
NL
/
PAISES BAJOS
/
THE NETHERLANDS