Smith T W, Wagner H
J Membr Biol. 1975;25(3-4):341-60. doi: 10.1007/BF01868583.
Antibodies have been obtained that specifically interact with the transport enzyme (Na+ + K+)-activated ATPase. The antigen used was purified (Na+ + Ka+)-ATPase from canine renal medulla. Purified gamma globulin from immunized animals, but not from control animals or preimmune serum, inhibited (Na+ + Ka+)-ATPase from canine renal medullar with reduction of activity to 33 +/- 4 (SD)% in concentration-dependent manner. Maximum inhibition occurred in less than 5 minutes at 37 degrees C. The Mg++ -dependent, nonouabain inhibited component of activity (Mg++ -ATPase) was unaffected. Fab fragments obtained by papain cleavage of the gamma globulin fraction had similar inhibitory activity and specificity. These antibodies also produced varying degrees of concentration-related inhibition of canine myocardial, calf brain, and human red cell ghost (Na++ + Ka+)-ATPase, but not Mg++-ATPase activity.
已获得能与转运酶(Na⁺+K⁺)激活的ATP酶特异性相互作用的抗体。所用抗原是从犬肾髓质纯化的(Na⁺+K⁺)-ATP酶。来自免疫动物而非对照动物或免疫前血清的纯化γ球蛋白,以浓度依赖方式抑制犬肾髓质的(Na⁺+K⁺)-ATP酶,活性降低至33±4(标准差)%。在37℃下不到5分钟就出现最大抑制。Mg²⁺依赖的、不受哇巴因抑制的活性成分(Mg²⁺-ATP酶)不受影响。通过木瓜蛋白酶裂解γ球蛋白部分获得的Fab片段具有相似的抑制活性和特异性。这些抗体还对犬心肌、小牛脑和人红细胞膜(Na⁺+K⁺)-ATP酶产生不同程度的浓度相关抑制,但对Mg²⁺-ATP酶活性无抑制作用。