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• W2000996009 abstract "To determine whether the lectin-induced inhibition of plasma membrane 5′-nucleotidase resulted from direct interaction of the lectin with the enzyme or indirectly from a membranous change due to lectin binding to other membrane glycoproteins, the enzyme was purified and its sensitivity tested in the absence of other membrane components. A 5000 fold purification was achieved by solubilization in Lubrol PX followed by gel filtration (Sephadex G-100), anion exchange (DEAE-Biogel A) and selective adsorption (hydroxylapatite) chromatography. The purified enzyme was even more sensitive to inhibition by high concentrations of concanavalin A, wheat germ agglutinin or Rincinus communis agglutinin than was the membrane-bound enzyme indicating that inhibition is due to direct binding of the lectins to the glycoprotein enzyme itself. Divalent succinyl Con A inhibited neither form of the enzyme suggesting the need for crosslinking for inhibition by the native lectin. The purified enzyme could not be activated by low concentrations of lectins which stimulated the membrane bound enzyme." @default.
• W2000996009 created "2016-06-24" @default.
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• W2000996009 date "1977-03-01" @default.
• W2000996009 modified "2023-09-24" @default.
• W2000996009 title "Lectin-induced inhibition of plasma membrane 5′-nucleotidase: Sensitivity of purified enzyme" @default.
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• W2000996009 doi "https://doi.org/10.1016/0006-291x(77)91048-8" @default.
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