Chillar R K, Beutler E
Blood. 1976 Mar;47(3):507-12.
The concept that ouabain-sensitive membrane (Na+ + K+)-ATPase-generated adenosine diphosphate (ADP) preferentially serves as the substrate for the phosphoglycerate kinase (PGK) step of erythrocyte glycolysis has been reexamined. Membrane ATPase readily provides ADP for and utilizes ATP generated in the pyruvate kinase (PK) step and is ouabain sensitive. Earlier reports in the literature, which have suggested that in hemolysates the ATPase reaction facilitating the PK reaction is ouabain-insensitive, are reinterpreted: in crude hemolysates ADP generated in the "backward" PGK reaction can account for these data. We conclude that there is no convincing evidence of selective linkage of (Na+ + K+)-ATPase with the PGK reaction.
哇巴因敏感的膜（Na⁺ + K⁺）-ATP酶产生的二磷酸腺苷（ADP）优先作为红细胞糖酵解中磷酸甘油酸激酶（PGK）步骤的底物这一概念已被重新审视。膜ATP酶很容易为丙酮酸激酶（PK）步骤中产生的ATP提供ADP并利用该ATP，且对哇巴因敏感。文献中早期的报道表明，在溶血产物中促进PK反应的ATP酶反应对哇巴因不敏感，现对此进行重新解读：在粗制溶血产物中，“逆向”PGK反应产生的ADP可以解释这些数据。我们得出结论，没有令人信服的证据表明（Na⁺ + K⁺）-ATP酶与PGK反应存在选择性联系。
