Johnson J H, Crider B P
Veterans Administration Medical Center, Dallas, TX 75216.
Proc Natl Acad Sci U S A. 1989 Oct;86(20):7857-60. doi: 10.1073/pnas.86.20.7857.
Increased Na+,K+-ATPase activity observed after chronic ethanol consumption has been examined to determine whether the increase is due to changes in the kinetic properties of the enzyme or increases in the amount of enzyme in the membranes examined. In skeletal muscle and erythrocyte ghosts from rat, as well as from humans, increased Na+,K+-ATPase activity in ethanol-consuming individuals was not accompanied by an increase in the number of ouabain binding sites. In studies with intact human erythrocytes, similar ouabain-sensitive 22Na+ and 86Rb+ pumping rates were observed between normal and ethanol-consuming individuals and the Na+ to Rb+ pumping ratio was found to be 1.5 in all cases. However, ouabain-sensitive lactate plus Pi formation was increased in cells from alcoholic individuals. Thus these data suggest that increased enzyme activity may be due to a kinetic alteration of the Na+,K+-ATPase and that the enzyme may be less efficient in coupling ion pumping to ATP hydrolysis than the enzyme in normal cells.
长期摄入乙醇后观察到的钠钾ATP酶活性增加,已被研究以确定这种增加是由于该酶动力学特性的改变,还是所检测膜中酶量的增加。在大鼠以及人类的骨骼肌和红细胞膜中,饮酒个体的钠钾ATP酶活性增加并未伴随着哇巴因结合位点数量的增加。在对完整人类红细胞的研究中,正常个体和饮酒个体之间观察到类似的对哇巴因敏感的22Na+和86Rb+泵浦速率,并且在所有情况下钠到铷的泵浦比率均为1.5。然而,酒精性个体的细胞中对哇巴因敏感的乳酸加无机磷形成增加。因此,这些数据表明酶活性增加可能是由于钠钾ATP酶的动力学改变,并且该酶在将离子泵浦与ATP水解偶联方面可能比正常细胞中的酶效率更低。