Purification and Characterization of L-Phenylalanine Aminopeptidase from Chick-Pea Cotyledons (Cicer arietinum L.) | BenthamScience

Purification and Characterization of L-Phenylalanine Aminopeptidase from Chick-Pea Cotyledons (Cicer arietinum L.)

Author(s): Margarita Marinova, Alexander Dolashki, Florian Altenberend, Stefan Stevanovic, Wolfgang Voelter, Bozhidar Tchorbanov.

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 2 , 2009

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°C. The determined constant of specificity kcat/Km during hydrolysis of Nunsubstituted 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.

Keywords: Chick-pea cotyledons, aminopeptidase, kinetic analysis, antihypertensive peptides

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 16
ISSUE: 2
Year: 2009
Page: [207 - 212]
Pages: 6
DOI: 10.2174/092986609787316333
Price: $58

Article Metrics

PDF: 1