Protein & Peptide Letters 2009-01-01

Purification and characterization of L-phenylalanine aminopeptidase from chick-pea cotyledons (Cicer arietinum L.).

Margarita Marinova, Alexander Dolashki, Florian Altenberend, Stefan Stevanovic, Wolfgang Voelter, Bozhidar Tchorbanov

Index: Protein Pept. Lett. 16 , 207-212, (2009)

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Abstract

Chick-pea (Cicer arietinum L.) cotyledons are unique source of aminopeptidase - 8-9 U/g cotyledons was observed using L-leucine-p-nitroanilide as substrate. The aminopeptidase was purified (65 kDa, pI 4.8 ) reaching a specific activity of 220 U/mg at pH 7.0-7.2 and 35-40 degrees C. The determined constant of specificity k(cat)/K(m) during hydrolysis of N-unsubstituted amino acid-p-nitroanilides showed a decrease order: Phe>Leu>Pro>Ile>Val>Ala. The enzyme was strongly inhibited by p-chloromercuribenzoic acid as well as in a competitive rate by the antihypertensive peptides Ile-Pro-Pro and Val-Pro-Pro.