Conway R G, Tao M
J Biol Chem. 1981 Nov 25;256(22):11932-8.
The effect of 2,3-diphosphoglycerate (2,3-P2-glycerate) on the phosphorylation of spectrin in solution by purified membrane cyclic AMP-independent protein kinase and in membrane preparations by the endogenous kinase was investigated. 2,3-P2-Glycerate inhibited spectrin phosphorylation both in solution and in the intact membrane. Kinetic analyses showed that 2,3-P2-glycerate had no effect on the Km for ATP but appeared to lower the Vmax of the reaction. When the effect of 2,3-P2-glycerate was examined in the presence of varying concentrations of spectrin, competitive inhibition kinetics were obtained. Interestingly, low concentrations of 2,3-P2-glycerate were found to effect the release of the membrane kinase from erythrocyte membranes. This release reaction may be related to the ability of 2,3-P2-glycerate to interfere with the interaction between the kinase and spectrin. The data suggest the possibility that the kinase may be bound to spectrin in the erythrocyte membrane. 2,3-P2-glycerate also caused the solubilization of 3-phosphoglyceraldehyde dehydrogenase, but not of cyclic AMP-dependent protein kinase. Taken together, our data indicate that 2,3-P2-glycerate may have a regulatory role in membrane protein phosphorylation and also may regulate the extent of association of the kinase with the membrane.
研究了2,3 - 二磷酸甘油酸（2,3-P2-甘油酸）对纯化的膜环磷酸腺苷非依赖性蛋白激酶在溶液中以及内源性激酶在膜制剂中使血影蛋白磷酸化的影响。2,3-P2-甘油酸在溶液中和完整膜中均抑制血影蛋白磷酸化。动力学分析表明，2,3-P2-甘油酸对ATP的Km无影响，但似乎降低了反应的Vmax。当在不同浓度的血影蛋白存在下检测2,3-P2-甘油酸的作用时，得到了竞争性抑制动力学。有趣的是，发现低浓度的2,3-P2-甘油酸会影响膜激酶从红细胞膜上的释放。这种释放反应可能与2,3-P2-甘油酸干扰激酶与血影蛋白之间相互作用的能力有关。数据表明激酶可能与红细胞膜中的血影蛋白结合。2,3-P2-甘油酸还导致3-磷酸甘油醛脱氢酶溶解，但不导致环磷酸腺苷依赖性蛋白激酶溶解。综上所述，我们的数据表明2,3-P2-甘油酸可能在膜蛋白磷酸化中具有调节作用，并且还可能调节激酶与膜的结合程度。
