An alternative oxidase monoclonal antibody recognises a highly conserved sequence among alternative oxidase subunits

被引：32

作者：

Finnegan, PM ^{[1
]}

Wooding, AR ^{[1
]}

Day, DA ^{[1
]}

机构：

[1] Australian Natl Univ, Div Biochem & Mol Biol, Fac Sci, Canberra, ACT 0200, Australia

来源：

FEBS LETTERS | 1999年 / 447卷 / 01期

基金：

澳大利亚研究理事会;

关键词：

higher plant; protozoan parasite; mitochondrium; respiration; alternative oxidase; epitope;

D O I：

10.1016/S0014-5793(99)00259-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The alternative oxidase is found in the inner mitochondrial membranes of plants and some fungi and protists. A monoclonal antibody raised against the alternative oxidase from the aroid lily Sauromatum guttatum has been used extensively to detect the enzyme in these organisms. Using an immunoblotting strategy, the antibody binding site has been localised to the sequence RADEAHHRDVNH within the soybean alternative oxidase 2 protein. Examination of sequence variants showed that A2 and residues C-terminal to H7 are required for recognition by the monoclonal antibody raised against the alternative oxidase. The recognition sequence is highly conserved among all alternative oxidase proteins and is absolutely conserved in 12 of 14 higher plant sequences, suggesting that this antibody will continue to be extremely useful in studying the expression and synthesis of the alternative oxidase. (C) 1999 Federation of European Biochemical Societies.

引用

页码：21 / 24

页数：4

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