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来自昆虫中肠和马氏管的17 kDa液泡H(+)-ATP酶蛋白脂质亚基的序列

Sequence of a 17 kDa vacuolar H(+)-ATPase proteolipid subunit from insect midgut and Malpighian tubules.

作者信息

Pietrantonio P V, Gill S S

机构信息

Department of Entomology, University of California, Riverside 92521.

出版信息

Insect Biochem Mol Biol. 1993 Sep;23(6):675-80. doi: 10.1016/0965-1748(93)90041-p.

DOI:10.1016/0965-1748(93)90041-p
PMID:8353524
Abstract

A 0.4 kb polymerase chain reaction (PCR) product obtained from cDNA made from the midgut and Malpighian tubules of fifth instar larvae of Heliothis virescens was used to screen a larval midgut and Malpighian tubules cDNA library. Four clones were obtained, one of 1.9 kb and others of 1.4 kb. The 1.9 kb clone encodes a 17.2 kDa protein which is highly homologous to other vacuolar ATPases proteolipids. Putative N-glycosylation and DCCD binding sites were observed at amino acid residues 83 and 139, respectively.

摘要

从绿铃夜蛾五龄幼虫中肠和马氏管制备的cDNA中获得的一段0.4 kb聚合酶链式反应(PCR)产物,用于筛选幼虫中肠和马氏管cDNA文库。获得了4个克隆,一个为1.9 kb,其他为1.4 kb。1.9 kb的克隆编码一种17.2 kDa的蛋白质,该蛋白质与其他液泡型ATP酶蛋白脂质高度同源。在氨基酸残基83和139处分别观察到推定的N-糖基化和DCCD结合位点。

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引用本文的文献

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The vacuolar H+-ATPase: a universal proton pump of eukaryotes.液泡H⁺-ATP酶:真核生物的通用质子泵。
Biochem J. 1997 Jun 15;324 ( Pt 3)(Pt 3):697-712. doi: 10.1042/bj3240697.