H⁺,K⁺-ATP酶的结构研究：NH₂末端氨基酸序列的测定以及与Na⁺,K⁺-ATP酶的免疫交叉反应性
Structural studies on H+,K+-ATPase: determination of the NH2-terminal amino acid sequence and immunological cross-reactivity with Na+,K+-ATPase.
作者信息
Lane L K, Kirley T L, Ball W J
出版信息
Biochem Biophys Res Commun. 1986 Jul 16;138(1):185-92. doi: 10.1016/0006-291x(86)90264-0.
The NH2-terminal amino acid sequence of the 100 kilodalton subunit of porcine gastric H+,K+-ATPase has been determined to be YKAENYELYQVELGPGP. Although the NH2-terminal region of this protein is not similar to the same region of the lamb kidney Na+,K+-ATPase catalytic subunit, other regions of these ATPase proteins appear to be homologous. Both monoclonal and polyclonal antibodies raised to lamb kidney Na+,K+-ATPase and its alpha, but not beta, subunit cross-react with the 100 kilodalton protein of H+,K+-ATPase.
猪胃H⁺，K⁺ -ATP酶100千道尔顿亚基的氨基末端氨基酸序列已确定为YKAENYELYQVELGPGP。尽管该蛋白质的氨基末端区域与羊肾Na⁺，K⁺ -ATP酶催化亚基的相同区域不相似，但这些ATP酶蛋白质的其他区域似乎是同源的。针对羊肾Na⁺，K⁺ -ATP酶及其α亚基（而非β亚基）产生的单克隆抗体和多克隆抗体均与H⁺，K⁺ -ATP酶的100千道尔顿蛋白质发生交叉反应。
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