Purification of maize alcohol dehydrogenase-1 allozymes and comparison of their tryptic peptides

Abstract

Two naturally occurring allozymes of alcohol dehydrogenase-1 in maize have been purified to homogeneity. Specific activity, molecular weight and amino acid composition have been determined. The difference between these two allozymes was further studied by comparisons of tryptic peptides using a fingerprinting technique. Excellent maps were obtained which resolved 29 out of the 30 peptides which were maximally possible. These allozymes differ in one peptide, consistent with a single, charged amino acid replacement. These results are related to the differences which have been shown to exist between the genes which specify these two allozymes.