Effect of a heat-stable factor in human placenta on glucosylceramidase, glucosylsphingosine glucosyl hydrolase, and acid beta-glucosidase activities.
Clin Biochem
; 20(6): 429-33, 1987 Dec.
Article
en En
| MEDLINE
| ID: mdl-3124976
A new protein activator of glucosylceramidase has recently been found in human placenta. In the present work, it has been compared with a previously reported glucosylceramidase activator, the Gaucher factor. The two activators showed different properties. The Gaucher factor stimulated 100% the 4-methylumbelliferyl-beta-D-glucopyranoside hydrolysis while the placental factor inhibited it 50%. Furthermore, the placental factor neither decreased the Michaelis constant, Km, nor increased the degree of inactivation by conduritol-beta-epoxide as the Gaucher factor does. From these results it has been concluded that the two activators are different substances. The activating effect of the placental factor is specific for the hydrolysis of glucosylceramide; neither the hydrolysis of glucosylsphingosine nor that of the 4-methylumbelliferyl derivative are enhanced by this protein. Owing to its specificity and high level in a human tissue, the placental factor is likely to have a physiological role in the catabolism of glucosylceramide.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Placenta
/
Extractos de Tejidos
/
Beta-Glucosidasa
/
Glucosidasas
/
Glucosilceramidasa
Límite:
Humans
Idioma:
En
Revista:
Clin Biochem
Año:
1987
Tipo del documento:
Article
País de afiliación:
Italia
Pais de publicación:
Estados Unidos