Multiple Forms of the Constitutive Wheat Cinnamyl Alcohol Dehydrogenase

Three cinnamyl alcohol dehydrogenase (CAD) isoenzymes were separatedfrom etiolated wheat seedlings (Triticum aestivum L.) and examinedby native gel electrophoresis. Two of these enzymes (CAD-1 andCAD-2) were purified to apparent homogeneity. They exhibiteda marked difference in substrate affinity. On sodium dodecylsulphate-acrylamide gel the isolated isoenzymes showed onlyone protein band each with an M_r 45000 and 40000 daltons, respectively,whereas on native gel two bands were identified for each protein.Isoenzymes from a variety of diploid, tetraploid, and hexaploidwheats were compared. The results indicated that the CAD polymorphismcould be genetically determined. Key words: Cinnamyl alcohol dehydrogenase, lignin, Triticum aestivum L