Abstract
Alcohol dehydrogenase isozyme proteins were characterized by visualization on two dimensional polyacrylamide gels. Native first dimension electrophoresis separates isozymes by size and charge, while preserving enzyme activity and subunit interactions. SDS electrophoresis in the second dimension breaks subunit interactions and separates polypeptides primarily by molecular weight. Results revealed that ADH2 monomers are larger in molecular weight than ADH1 monomers. An EMS induced Adhl mutant was found to produce ADH1 monomers of reduced molecular weight. Autoradiography revealed that only a few proteins (five or six) including ADH1 and ADH2 actively incorporate labelled amino acids after prolonged anaerobiosis.
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