Properties of aminopeptidases from bean seeds

Blättler, R; Feller, Urs (June 1987). Properties of aminopeptidases from bean seeds. Experientia, 43(6), p. 659. Basel: Birkhäuser Verlag

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Aminopeptidase forms, extracted from ungerminated bean seeds (Phaseolus vulgar& L., var. 'Saxa'), were separated by ion exchange and gel chromatography. The activities were detected with the following L-amino acid-p-nitroanilides: gly, ala, lys, arg, leu, met and phe as substrates. Some properties of four forms differing in their substrate specificities (1: ala/lys/arg; 2: leu/met/phe; 3: gly; 4: phe) were further investigated. The pHoptima were broad and similar for forms 1 and 2 (around pH 7.25), while gly was most rapidly liberated about pH 8.0 and form 4 was most active around pH 7.0. The form liberating ala, lys and arg was highly sensitive to 1,10-phenanthroline, but the same concentration of this chelator had no major effect on the other forms. The activities of forms 2, 3 and 4 decreased after addition of MgC12, while form '1 was more tolerant in this respect. The inactivation of forms 1,2 and 3 was accelerated by the addition of endopeptidases. The form acting on phe was less sensitive to these treatments.

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