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  • Characterization of an aminopeptidase and a proline iminopeptidase from cabbage leaves.

Characterization of an aminopeptidase and a proline iminopeptidase from cabbage leaves.

Zeitschrift fur Naturforschung. C, Journal of biosciences (2008-04-05)
Margarita Marinova, Alexander Dolashki, Florian Altenberend, Stefan Stevanovic, Wolfgang Voelter, Bozhidar Tchorbanov
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 for aminopeptidase activity and 8.0-8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase-associated protein (approximately 70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33).

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Sigma-Aldrich
L -脯氨酸对硝基苯胺 三氟乙酸盐, prolyl aminopeptidase substrate