Abstract
A novel aspartic proteinase (EC 3.4.23) from Medicago sativa L. (alfalfa) was purified to homogeneity using Source Q ion-exchange, concanavalin-A Sepharose and pepstatin-A agarose affinity chromatography. The enzyme, M r=33.5 kDa, is monomeric and catalyzes the cleavage of a broad spectrum of peptide bonds of hydrophobic amino acids from pH 2.6 to 6.4. The enzyme is inhibited by pepstatin-A and is consistent with the properties of an aspartic proteinase. The N-terminal amino acid sequence of the protein shows 50 and 40% similarity with the cyprosin and barley aspartic proteinases, respectively.
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Payie, K.G., Weadge, J.T., Tanaka, T. et al. Purification, N-terminal sequencing and partial characterization of a novel aspartic proteinase from the leaves of Medicago sativa L. (alfalfa). Biotechnology Letters 22, 1515–1520 (2000). https://doi.org/10.1023/A:1005656208075
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DOI: https://doi.org/10.1023/A:1005656208075