Abstract
An aminopeptidase was purified from buckwheat seed by using affinity chromatography, ion-exchange chromatography and chromatofocusing. The enzyme had a molecular weight of 37,000 as determined by gel filtration. The aminopeptidase activity, determined with l-leucine-p-nitroanilide (Leu-pNA) as the substrate, exhibited a pH optimum of 7.2. The Km value for Leu-pNA was 140 μm. The preferred substrates were l-leucine-β-naphtylamide and Leu-pNA, although there was also high activity against l-leucyl-l-alanine and l-leucinamide. Thiol antagonists were found to be potent inhibitors against the enzyme. The enzyme exhibited less or no sensitivity to the endogeneous proteinase inhibitors, benzamidine and TPCK.
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