Boldyrev A A
Department of Biochemistry, School of Biology, Moscow State University, USSR.
Acta Physiol Pharmacol Bulg. 1988;14(2):3-9.
Some kinetic features of transport ATPases (Na, K-dependent and Ca-dependent) are characterized. The experimental data point to the existence of cooperative interactions between functional units of transport ATPases in membrane matrix. Detergent treatment showed that cooperativity with respect to the substrate is realized via interactions between several functional units (protomers), whereas cooperativity with respect to activating ions is manifested at the ion-binding sites of each protomer of transport ATPases. Structural changes in the ATPase molecules which reflect interprotein interactions induced by high ATP concentration have been revealed.
对转运ATP酶（钠钾依赖型和钙依赖型）的一些动力学特征进行了表征。实验数据表明，膜基质中转运ATP酶的功能单元之间存在协同相互作用。去污剂处理表明，底物协同性是通过几个功能单元（原体）之间的相互作用实现的，而激活离子的协同性则在转运ATP酶每个原体的离子结合位点上表现出来。已经揭示了ATP酶分子中的结构变化，这些变化反映了高ATP浓度诱导的蛋白质间相互作用。
