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
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
.