Garner M H, Spector A
Biochem Biophys Res Commun. 1985 Sep 30;131(3):1206-11. doi: 10.1016/0006-291x(85)90219-0.
The kinetics of hydrolysis of ATP were determined for the renal Na,K-ATPase, in the K+ conformation, modified with glucose-6-phosphate. There was a shift in the ATP hydrolysis kinetics from negative kinetic co-operativity for the control enzyme preparations to substrate inhibition kinetics for the modified enzyme preparations. The effect was reversible and stabilized after NaBH4 reduction. Approximately 4 moles of glucose-6-phosphate were incorporated per mole of Na,K-ATPase (based on MW of 150,000 daltons). Similar substrate inhibition kinetics were observed for the renal Na,K-ATPase isolated from several human subjects with mature onset diabetes.
测定了用6-磷酸葡萄糖修饰的处于K⁺构象的肾钠钾ATP酶的ATP水解动力学。ATP水解动力学发生了变化,从对照酶制剂的负协同动力学转变为修饰酶制剂的底物抑制动力学。该效应是可逆的,在硼氢化钠还原后得以稳定。每摩尔钠钾ATP酶(基于150,000道尔顿的分子量)约结合4摩尔6-磷酸葡萄糖。从几名成年发病型糖尿病患者分离出的肾钠钾ATP酶也观察到了类似的底物抑制动力学。