Polymorphism of the cobalt-activated acylase in human tissues.
Acta Biochim Pol
; 25(1): 3-14, 1978.
Article
en En
| MEDLINE
| ID: mdl-27051
ABSTRACT
A method was elaborated for obtaining polyacrylamide gel zymograms of the cobalt-activated acylase after electrophoresis. Two fractions of the acylase showing activity towards N-chloroacetyl-gamma-L-glutamyl-beta-naphthylamide were found in human kidney, liver and intestine. The two fractions isolated from liver differ in substrate specificity, heat resistance, response to metal ions, inhibition by deaminated dipeptides, and in molecular weight. They differ also from other N-acylamino acid amidohydrolases aminoacylase (EC 3.5.1.14) and aspartoacylase (EC 3.5.1.15).
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Bases de datos:
MEDLINE
Asunto principal:
Aminopeptidasas
Límite:
Humans
Idioma:
En
Revista:
Acta Biochim Pol
Año:
1978
Tipo del documento:
Article