Averdunk R, Müller J, Wenzel B
J Clin Chem Clin Biochem. 1976 Jul;14(7):339-44.
The ouabain-sensitive and ouabain-intensitive ATP-ases of intact lymphocytes, and of the lymphocyte microsomal fraction and a purified plasma membrane fraction, are all activated by concanavalin A. The Na+, K+, and Mg+-dependence of the plasma membrane ATP-ases were defined at different substrate concentrations. Enzyme activation was rather greater at lower K+ concentrations. From these studies it appears improbable, but not impossible, that concanavalin A exerts an allosteric effect on the ATP-ases.
完整淋巴细胞、淋巴细胞微粒体部分及纯化质膜部分的哇巴因敏感型和哇巴因不敏感型ATP酶均被伴刀豆球蛋白A激活。在不同底物浓度下确定了质膜ATP酶对Na⁺、K⁺和Mg⁺的依赖性。在较低K⁺浓度下酶激活作用更强。从这些研究来看,伴刀豆球蛋白A对ATP酶产生变构效应似乎不太可能,但并非没有可能。