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5'-Nucleotidase activity of lymphocyte plasma membranes. Effect of concanavalin A]
Authors:J Dornand  C Réminiac  J C Mani
Affiliation:ER CNRS n° 62, Ecole Nationale Supérieure de Chimie, 8, rue de l''Ecole Normale, 34075 Montpellier Cedex, France
Abstract:The 5'-nucleotidase properties of isolated lymphocyte plasma membranes from young pig mesenteric nodes are described; nucleosides-5'-monophosphates are the substrates of this specific enzyme. Concanavalin A inhibits this enzyme; on the same membranes this mitogen does not affect alkaline phosphatase and activates the membrane bound (Ca2+) ATPase. The 5'-nucleotidase inhibition is due to a specific interaction of Con A with carbohydrate groups of the membrane; its high positive cooperativity suggests that the lectin promotes reorganization of the membrane bound 5'-nucleotidase. Solubilization of the 5'-nucleotidase does not prevent the effect of Con A and the solubilized enzyme is firmly bound by Con A-Sepharose 4B; these results suggest that Con A inhibits the enzyme by a direct interaction and that 5'-nucleotidase can be considered as an eventual receptor for the lectin.
Keywords:5′-AMP  5′-adénosine monophosphate  5′-CMP  5′-cytosine monophosphate  5′-GMP  5′-guanosine monophosphate  5′-IMP  5′-inosine monophosphate  5′-dAMP  5′-désoxyadénosine monophosphate  5′-dCMP  5′-désoxycytosine monophosphate  PNP  paranitrophénol  PNPP  paranitrophényl phosphate  DOC  désoxycholate de sodium  Con A  concanavaline A  Pi  phosphate inorganique  TCA  acide trichloracétique  EDTA  acide éthylène-diamine-tétraacétique  EGTA  acide éthylèneglycol-bis-(2-aminoéthyl)- té-traacétique
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