Abstract
Two anodic isoperoxidases (A 1 and A 2) from tobacco tissue culture W-38 and two cathodic isoperoxidases (C 3 and C 4) from tobacco suspension culture WR-132 have been separated and characterized. Molecular weights for each of the isoperoxidases have been determined by two different methods. Only C 4 contained a carbohydrate component. The substrate specificity and the pH optima for the four enzymes with each of five substrates were determined.
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