Purification of a heterodimeric betaine aldehyde dehydrogenase from wild amaranth plants subjected to water deficit

被引：7

作者：

Figueroa-Soto, CG ^{[1
]}

Valenzuela-Soto, EM ^{[1
]}

机构：

[1] Ctr Invest Aliment & Desarrollo AC, Direcc Ciencia Alimentos, Hermosillo 83100, Sonora, Mexico

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2001年 / 285卷 / 04期

关键词：

betaine aldehyde dehydrogenase; glycine betaine; water deficit; heat shock proteins; wild plants;

D O I：

10.1006/bbrc.2001.5286

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：

Betaine aldehyde dehydrogenase was purified to homogeneity from wild-type amaranth plants subjected to water deficit. The enzyme has a native molecular mass of 125 kDa; it is formed by two subunits, one of the subunits with a molecular mass of 63 kDa and the second one of 70 kDa as determined by SDS-PAGE and double dimension electrophoresis. IEF studies showed two bands with pl values of 4.93 and 4.85, respectively. Possible glycosilation of the 63- and 70-kDa subunits were tested with negative results. Both subunits crossreacted strongly with polyclonal antibody raised against porcine kidney BADH. Also antiserum rose against HSP70 cross-reacted strongly with the wild amaranth BADH 70-kDa subunit. The enzyme was stable to extreme pH's and temperatures, and high KCI concentrations. Product inhibition of BADH was not observed. (C) 2001 Academic Press.

引用

页码：1052 / 1058

页数：7

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