Chetty C S, Rajanna B, Rajanna S
Department of Natural Sciences, Selma University, AL 36701.
Toxicol Lett. 1990 Mar;51(1):109-16. doi: 10.1016/0378-4274(90)90230-j.
This study concerned the effects of mercuric chloride on Na+/K(+)-ATPase and [3H]ouabain binding in rat brain microsomes in vitro. The data showed that HgCl2 inhibited Na+/K(+)-ATPase effectively at micromolar concentrations. The degree of inhibition was decreased with increases in enzyme concentration and incubation time. Variations in the ionic strength of Na+ and K+ did not alter the percent inhibition of Na+/K(+)-ATPase activity by HgCl2. Repeated washings partially restored enzyme activity. The binding of [3H]ouabain to microsomal membranes was inhibited by HgCl2 in a concentration-dependent manner. Cumulative inhibition studies with HgCl2 and ouabain indicated that these inhibitors did not act concurrently and independently on Na+/K(+)-ATPase.
本研究关注氯化汞对大鼠脑微粒体中Na⁺/K⁺-ATP酶及[³H]哇巴因结合的体外效应。数据表明,氯化汞在微摩尔浓度时能有效抑制Na⁺/K⁺-ATP酶。抑制程度随酶浓度和孵育时间的增加而降低。Na⁺和K⁺离子强度的变化并未改变氯化汞对Na⁺/K⁺-ATP酶活性的抑制百分比。反复洗涤可部分恢复酶活性。[³H]哇巴因与微粒体膜的结合受到氯化汞浓度依赖性抑制。氯化汞与哇巴因的累积抑制研究表明,这些抑制剂并非同时且独立地作用于Na⁺/K⁺-ATP酶。