ISSN:
0091-7419
Schlagwort(e):
Life Sciences
;
Molecular Cell Biology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Biologie
,
Chemie und Pharmazie
,
Medizin
Notizen:
The plant lectin concanavalin A (Con A) specifically inactivates the 5′ -nucleotidase of a plasma membrane-enriched fraction from lactating mammary gland. The lectin also causes an activation of the membrane Mg++ -ATPase, but does not affect galactosyltransferase or alkaline phosphatase. The enzyme perturbations are prevented by α-methylmannoside, an inhibitor of Con A binding, indicating that specific binding to carbohydrate structures rather than nonspecific protein-protein interaction is involved. Solubilization of the 5′ -nucleotidase in detergents (0.2% Triton X-100 or 1% deoxycholate) does not prevent Con A inactivation, indicating that incorporation into the membrane structure is not a requirement for the Con A effect. The results suggest that Con A inactivates the 5′ -nucleotidase by a direct interaction with the enzyme and that this enzyme is a Con A receptor site on the surface of mammary cells.
Zusätzliches Material:
1 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/jss.400040111
