Purification and characterization of variant alcohol dehydrogenase isozymes from durum wheat
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- Suseelan, K.N., Mitra, R. & Bhatia, C.R. Biochem Genet (1987) 25: 581. doi:10.1007/BF00554359
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Three alcohol dehydrogenase (ADH) isozymes from embryos of the durum wheat cultivar Bijaga Yellow having the variantAdh-Alb allele were purified using (NH4)2SO4 precipitation, gel filtration, and ion-exchange chromatography. ADH is a dimeric enzyme. The variant isozyme ADH-1-1, which is a homodimer composed of αb monomers, was compared with ADH-1-5 (homodimer composed of βa monomers), the product ofAdh-B1, and the ADH-1-3 isozyme (αbβa heterodimer) on a number of parameters includingKm, substrate specificities, and molecular weights. No appreciable differences among the three isozymes were found, except for the faster electrophoretic mobility of αbαb dimers (ADH-1-1). The results indicate that the variant isozyme is the result of a mutation altering only the charge of the isozyme.