Purification, N-terminal sequencing and partial characterization of a novel aspartic proteinase from the leaves of Medicago sativa L. (alfalfa)

Citation
Kg. Payie et al., Purification, N-terminal sequencing and partial characterization of a novel aspartic proteinase from the leaves of Medicago sativa L. (alfalfa), BIOTECH LET, 22(19), 2000, pp. 1515-1520
Citations number
15
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
BIOTECHNOLOGY LETTERS
ISSN journal
01415492 → ACNP
Volume
22
Issue
19
Year of publication
2000
Pages
1515 - 1520
Database
ISI
SICI code
0141-5492(200010)22:19<1515:PNSAPC>2.0.ZU;2-X
Abstract
A novel aspartic proteinase (EC 3.4.23) from Medicago sativa L. (alfalfa) w as purified to homogeneity using Source Q ion-exchange, concanavalin-A Seph arose and pepstatin-A agarose affinity chromatography. The enzyme, M-r=33.5 kDa, is monomeric and catalyzes the cleavage of a broad spectrum of peptid e bonds of hydrophobic amino acids from pH 2.6 to 6.4. The enzyme is inhibi ted by pepstatin-A and is consistent with the properties of an aspartic pro teinase. The N-terminal amino acid sequence of the protein shows 50 and 40% similarity with the cyprosin and barley aspartic proteinases, respectively .