Anner B M, Lane L K, Schwartz A, Pitts B J
Biochim Biophys Acta. 1977 Jun 16;467(3):340-5. doi: 10.1016/0005-2736(77)90311-x.
Liposomes containing either purified or microsomal (Na+,K+)-ATPase preparations from lamb kidney medulla catalyzed ATP-dependent transport of Na+ and K+ with a ratio of approximately 3Na+ to 2K+, which was inhibited by ouabain. Similar results were obtained with liposomes containing a partially purified (Na+,K+)-ATPase from cardiac muscle. This contrasts with an earlier report by Goldin and Tong (J. Biol. Chem. 249, 5907-5915, 1974), in which liposomes containing purified dog kidney (Na+,K+)-ATPase did not transport K+ but catalyzed ATP-dependent symport of Na+ and Cl-. When purified by our procedure, dog kidney (Na+,K+)-ATPase showed some ability to transport K+ but the ratio of Na+ : K+ was 5 : 1.
含有从羊肾髓质中提取的纯化或微粒体(Na⁺,K⁺)-ATP酶制剂的脂质体催化了Na⁺和K⁺的ATP依赖性转运,其比例约为3个Na⁺比2个K⁺,且该转运被哇巴因抑制。含有从心肌中提取的部分纯化的(Na⁺,K⁺)-ATP酶的脂质体也得到了类似结果。这与戈尔丁和汤(《生物化学杂志》249卷,5907 - 5915页,1974年)早期的一份报告形成对比,在该报告中,含有纯化的狗肾(Na⁺,K⁺)-ATP酶的脂质体不转运K⁺,而是催化Na⁺和Cl⁻的ATP依赖性同向转运。当按照我们的方法进行纯化时,狗肾(Na⁺,K⁺)-ATP酶显示出一定的转运K⁺的能力,但Na⁺:K⁺的比例为5:1。