Boldyrev A, Kurella E
International Biotechnological Center, Moscow State University, Russia.
Biochem Biophys Res Commun. 1996 May 15;222(2):483-7. doi: 10.1006/bbrc.1996.0770.
Oxidative modification of kidney Na/K-ATPase was found to be accompanied by a decrease in the amount of sulfhydryl groups accessible for Elmann reagent with subsequent transformation of kinetic behavior of the enzyme. Oxidation of Na/K-ATPase with 20 mM hydrogen peroxide during 20 min results in about 50% inhibition of its activity and subsequent transformation of complex substrate-velocity dependence into the simple hyperbolic curve. In terms of kinetic analysis the suggestion was made that partial oxidation of Na/K-ATPase by hydrogen peroxide results in disordering of interprotomer interaction in the oligomeric complex of Na/K-ATPase.
已发现肾脏钠钾ATP酶的氧化修饰伴随着可被埃尔曼试剂检测到的巯基数量的减少,随后酶的动力学行为发生转变。在20分钟内用20 mM过氧化氢氧化钠钾ATP酶,导致其活性约50%受到抑制,随后复杂的底物-速度依赖性转变为简单的双曲线。从动力学分析来看,有人提出过氧化氢对钠钾ATP酶的部分氧化导致了钠钾ATP酶寡聚体复合物中原聚体间相互作用的紊乱。