[Electrophoretic analysis of substrate specificity of wheat alcohol dehydrogenases].
Electrophoresis in polyacrylamide gel slabs has been used to study the isoform composition and substrate specificity of alcohol dehydrogenases in the embryo and young seedlings of the diploid wheat Triticum monococcum L., the tetraploid T. dicoccon (Schrank) Schuebl and the hexaploid T. spelta L. Three alcohol dehydrogenases of different substrate specificity and developmental pattern were distinguished: a) the NAD-dependent alcohol dehydrogenase, catalyzing the oxidation of different primary and secondary aliphatic and aromatic alcohols, as well as certain compounds with several hydroxyl groups (tris, triethanolamin) and revealing, after electrophoresis, one major band in the diploid wheat and three bands in both polyploid wheats; b) the NADP-dependent aromatic alcohol dehydrogenase (substrate--cinnamic alcohol), revealing, after electrophoresis, one major fast moving band in the diploid wheat and two bands in polyploid wheats; c) an aromatic alcohol dehydrogenase (2-3 bands after electrophoreis) with no specificity to the cofactors (NAD or NADP).
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D009243:NAD; D009249:NADP; D010636:Phenols; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity; D014908:Triticum / Q000201:enzymology
D010636:Phenols; D009243:NAD; D009249:NADP; D000429:Alcohol Oxidoreductases
Elektroforeticheskiĭ analiz substrathoĭ spetsifichnosti alkogol'degidrogenaz pshenitsy.