Gerencser G A
Department of Physiology, College of Medicine, JHMHC, University of Florida, Gainesville 32610.
Biochim Biophys Acta. 1990 Apr 30;1023(3):475-7. doi: 10.1016/0005-2736(90)90142-b.
A Cl(-)-stimulated ATPase activity, which is sensitive to both N-ethylmaleimide and p-chloromercuribenzenesulfonate, has been localized to the basolateral membrane of Aplysia enterocytes. Dithiothreitol reversed the inhibition of Cl(-)-stimulated ATPase induced by p-chloromercuribenzenesulfonate. These results suggest that surface sulfhydryl ligands of the ATPase participate in the catalytic activity of the enzyme.
一种对N-乙基马来酰亚胺和对氯汞苯磺酸盐均敏感的Cl(-)刺激型ATP酶活性，已定位到海兔肠上皮细胞的基底外侧膜。二硫苏糖醇可逆转对氯汞苯磺酸盐对Cl(-)刺激型ATP酶的抑制作用。这些结果表明，该ATP酶的表面巯基配体参与了酶的催化活性。
