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Purification and partial characterization of Phaseolus vulgaris seed aminopeptidase BJMBR
Abdala,A.P.; Takeda,L.H.; Freitas Jr.,J.O.; Alves,K.B..
The aminopeptidase activity of Phaseolus vulgaris seeds was measured using L-Leu-p-nitroanilide and the L-aminoacyl-ß-naphthylamides of Leu, Ala, Arg and Met. A single peak of aminopeptidase activity on Leu-ß-naphthylamide was eluted at 750 µS after gradient elution chromatography on DEAE-cellulose of the supernatant of a crude seed extract. The effluent containing enzyme activity was applied to a Superdex 200 column and only one peak of aminopeptidase activity was obtained. SDS-polyacrylamide gel electrophoresis (10%) presented only one protein band with molecular mass of 31 kDa under reducing and nonreducing conditions. The aminopeptidase has an optimum pH of 7.0 for activity on all substrates tested and the highest Vmax/KM ratio for...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Phaseolus vulgaris aminopeptidase; Bean seed aminopeptidase; Leucyl aminopeptidase.
Ano: 1999 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999001200006
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