Ottolenghi P
Biochem J. 1975 Oct;151(1):61-6. doi: 10.1042/bj1510061.
A microsomal fraction rich in Na+, K+-ATPase (sodium-plus-potassium ion-dependent adenosine triphosphatase) and the corresponding K+-dependent p-nitrophenyl phosphatase from the rectal salt gland of the spiny dogfish was solubilized by treatment with deoxycholate at high ionic strength. On gel filtration through Sepharose 6B, the ATPase apoenzyme could be separated, in apparently soluble form, from the tissue-fraction phospholipids and was almost free of enzymic activity (2% of the p-nitrophenyl phosphatase activity and 0.2% of the ATPase activity being recovered). On mixing the apoenzyme with an activator consisting of cooked ox brain, a large proportion of the original enzymic activity was obtained. Specific activities of the re-activated enzyme were somewhat higher than in the material before gel filtration: values of 1300-1450 mumol and 250-290 mumol/h per mg of protein were obtained for the hydrolysis of ATP and of p-nitrophenyl phosphate respectively. The activity was inhibitible by ouabain.
用高离子强度的脱氧胆酸盐处理多刺角鲨直肠盐腺中富含Na⁺、K⁺-ATP酶（钠钾离子依赖性三磷酸腺苷酶）及相应的钾依赖性对硝基苯磷酸酶的微粒体部分，可使其溶解。通过琼脂糖6B凝胶过滤，ATP酶脱辅基酶可从组织部分磷脂中以明显可溶的形式分离出来，且几乎没有酶活性（回收的对硝基苯磷酸酶活性为2%，ATP酶活性为0.2%）。将脱辅基酶与由煮熟的牛脑组成的激活剂混合后，可获得很大比例的原始酶活性。再激活酶的比活性略高于凝胶过滤前的物质：每毫克蛋白质水解ATP和对硝基苯磷酸的速率分别为1300 - 1450 μmol/h和250 - 290 μmol/h。该活性可被哇巴因抑制。
