Abstract
Two aminotransferases present in crude extracts of mustard seedling cotyledons were separated into isoforms using a Mono Q ion-exchange column. Four isoenzymes of aspartate aminotransferase were found, three of which were constitutively expressed. Only the predominant isoform exhibited changes in enzyme level that depended on plastidic factor and the nitrogen source. In comparison, alanine aminotransferase appeared to be regulated by light and the plastidic factor. After chromatographic separation, four isoforms of the enzyme were detected. The subcellular localization of these isoforms and their regulation are discussed.
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