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)
Full Text: HTML
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.
Related Compounds
Related Articles:
2014-08-01
[Appl. Microbiol. Biotechnol. 98(15) , 6689-700, (2014)]
2015-01-01
[Nat. Prod. Res. 29 , 1650-6, (2015)]
2009-11-01
[Microbiology 155 , 3673-3682, (2009)]
Characterization of an aminopeptidase and a proline iminopeptidase from cabbage leaves.
2008-01-01
[Z. Naturforsch., C, J. Biosci. 63 , 105-112, (2008)]
Collagen production in cardiac fibroblasts during inhibition of aminopeptidase B.
2005-09-01
[J. Renin Angiotensin Aldosterone Syst. 6 , 69-77, (2005)]