Inhibition of 5'-nucleotidase by concanavalin A: evidence for localization on the outer surface of the plasma membrane

5'-Nucleotidase activity of rat liver plasma membrane is markedly inhibited by concanavalin A. Taken together with a unilateral pattern of labelling of concanavalin A binding sites with hemocyanin, the results indicate that an allosteric site of the enzyme is at the outer surface of the membran...

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Bibliographic Details
Published in:Cell and tissue research 1976-08, Vol.170 (4), p.477-484
Main Authors: Williamson, F A, Morré, D J, Shen-Miller, J
Format: Article
Language:English
Subjects:
Allosteric Site
Animals
Binding Sites, Antibody
Cell Membrane - analysis
Cell Membrane - ultrastructure
Concanavalin A - pharmacology
Hemocyanins
Nucleotidases - analysis
Nucleotidases - antagonists & inhibitors
Rats
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Summary:5'-Nucleotidase activity of rat liver plasma membrane is markedly inhibited by concanavalin A. Taken together with a unilateral pattern of labelling of concanavalin A binding sites with hemocyanin, the results indicate that an allosteric site of the enzyme is at the outer surface of the membrane.
ISSN:0302-766X
1432-0878
DOI:10.1007/BF00361705