Purification of a heterodimeric betaine aldehyde dehydrogenase from wild amaranth plants subjected to water deficit.
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 pI values of 4.93 and 4.85, respectively. Possible glycosilation of the 63- and 70-kDa subunits were tested with negative results. Both subunits cross-reacted 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 KCl concentrations. Product inhibition of BADH was not observed.
Figueroa-Soto
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CG
Dirección de Ciencia de los Alimentos, Centro de Investigación en Alimentación y Desarrollo A.C., Hermosillo, Sonora, CP 83100, México.
Valenzuela-Soto
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EM
D000220:Adaptation, Biological / Q000502:physiology*; D000445:Aldehyde Oxidoreductases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D050728:Betaine-Aldehyde Dehydrogenase; D003429:Cross Reactions; D003889:Desert Climate; D019281:Dimerization; D018840:HSP70 Heat-Shock Proteins / Q000276:immunology; D019684:Magnoliopsida / Q000201:enzymology*; D009997:Osmotic Pressure; D018515:Plant Leaves / Q000201:enzymology; D012621:Seasons; D013045:Species Specificity; D013379:Substrate Specificity; D014867:Water / Q000378:metabolism*
D018840:HSP70 Heat-Shock Proteins; D014867:Water; D000445:Aldehyde Oxidoreductases; D050728:Betaine-Aldehyde Dehydrogenase