PURIFICATION AND PARTIAL SEQUENCE-ANALYSIS OF PLANT ANNEXINS

被引：56

作者：

SMALLWOOD, M ^{[1
]}

KEEN, JN ^{[1
]}

BOWLES, DJ ^{[1
]}

机构：

[1] UNIV LEEDS,DEPT BIOCHEM,WOODHOUSE LANE,LEEDS LS2 9JT,W YORKSHIRE,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1990年 / 270卷 / 01期

关键词：

D O I：

10.1042/bj2700157

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：

A fractionation procedure for annexins involving Ca2+-dependent binding to exogenous phospholipid was applied to tomato suspension culture cells. Two polypeptides (34 kDa and 35.5 kDa) were purified and separated from each other and from contaminant pectic polysaccharide by ion-exchange chromatography. After proteolytic digestion of SDS/PAGE-purified products, N-terminal sequencing of the peptide fragments revealed substantial similarity to sequences of known members of the annexin family characterized from a range of animal tissues. In particular, sequence similarity to the 70-amino acid-residue repeat region found in all annexins sequenced to date was present in both of the plant proteins. The data are discussed within the context of annexin involvement in Ca2+-mediated events in higher plants.

引用

页码：157 / 161

页数：5

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