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牛嗜铬细胞液泡ATP酶亚基A的结构与表达

Structure and expression of subunit A from the bovine chromaffin cell vacuolar ATPase.

作者信息

Pan Y X, Xu J, Strasser J E, Howell M, Dean G E

机构信息

Department of Physiology and Biophysics, University of Cincinnati College of Medicine, OH 45267-0524.

出版信息

FEBS Lett. 1991 Nov 18;293(1-2):89-92. doi: 10.1016/0014-5793(91)81158-5.

Abstract

Subunit A of the vacuolar H(+)-ATPase class is thought to be responsible for the ATP hydrolysis which drives proton-pumping. We report here the cloning and sequence determination of the first mammalian cDNA encoding a bovine vacuolar ATPase subunit A from an adrenal medulla cDNA library. Northern blots of bovine adrenal medulla RNA reveal a message of approximately 3.8 kb. The predicted peptide sequence, consisting of 618 amino acids with a calculated molecular weight of 68397 daltons, is similar to the sequences of the three known subunit A proteins. beta-Galactosidase-subunit A fusion proteins were immuno-decorated by an antiserum raised to the subunit A protein from corn coleoptile vacuoles.

摘要

液泡H(+)-ATP酶A亚基被认为负责驱动质子泵的ATP水解。我们在此报告从肾上腺髓质cDNA文库中克隆并测序了首个编码牛液泡ATP酶A亚基的哺乳动物cDNA。牛肾上腺髓质RNA的Northern印迹显示出一条约3.8 kb的信息。预测的肽序列由618个氨基酸组成,计算分子量为68397道尔顿,与三种已知的A亚基蛋白序列相似。β-半乳糖苷酶-A亚基融合蛋白被针对玉米胚芽鞘液泡A亚基蛋白产生的抗血清免疫标记。

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