Carraway C A, Carraway K L
J Supramol Struct. 1976;4(1):121-6. doi: 10.1002/jss.400040111.
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 alpha-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.
植物凝集素伴刀豆球蛋白A（Con A）能特异性地使来自泌乳乳腺富含质膜的部分中的5'-核苷酸酶失活。该凝集素还会引起膜Mg++-ATP酶的激活，但不影响半乳糖基转移酶或碱性磷酸酶。α-甲基甘露糖苷（Con A结合的抑制剂）可防止酶的扰动，这表明涉及与碳水化合物结构的特异性结合而非非特异性蛋白质-蛋白质相互作用。在去污剂（0.2% Triton X-100或1%脱氧胆酸盐）中溶解5'-核苷酸酶并不能阻止Con A使其失活，这表明整合到膜结构中并非Con A发挥作用的必要条件。结果表明，Con A通过与该酶直接相互作用使5'-核苷酸酶失活，并且这种酶是乳腺细胞表面的一个Con A受体位点。
