Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves
作者： Margarita Marinova , Alexander Dolashki , Florian Altenberend , Stefan Stevanovic , Wolfgang Voelter
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摘要: Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2-7.5 aminopeptidase activity 8.0-8.5 iminopeptidase determined. Both peptidases strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions urea. The molecular weights determined gel filtration to be 56 204 kDa, respectively. was decomposed during SDS electrophoresis four subunits of 50 kDa. Minor impurities myrosinase-associated protein (approximately 70 kDa) found in both preparations. Preliminary data their amino acid sequences showed similarities those aminopeptidases N (family M1) iminopeptidases S33).
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