Purification and some properties of buffalo spleen cathepsin Β.
J Biosci
;
1989 Sep; 14(3): 261-268
Article
Dans Anglais
| IMSEAR
| ID: sea-160737
ABSTRACT
Purification of cathepsin Β from buffalo-spleen, a hitherto unstudied system has been achieved by a simple procedure developed by incorporating suitable modifications in the existing methods for isolation of the enzyme from other sources. The purified enzyme has a molecular weight of 25 KDa and its Stokes radius was found to be 2·24 nm. Effects of several reducing agents, urea and thiol-protease inhibitors such as leupeptin and antipain, have been studied and the data unequivocally support the contention that the buffaloenzyme is similar to cathepsin Β from other tissues with respect to these properties.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
langue:
Anglais
Texte intégral:
J Biosci
Année:
1989
Type:
Article
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