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  • Title: [Partial purification and characterization of protease A of germinating vetch seeds, hydrolyzing native reserve proteins].
    Author: Bul'maga VP, Shutov AD.
    Journal: Biokhimiia; 1977 Nov; 42(11):1983-9. PubMed ID: 588633.
    Abstract:
    Protease A is 870-fold purified by means of isoelectric precipitation, DEAE-cellulose chromatography and gel filtration through Sephadex G-50, the yield of the enzyme being 28%. The purified preparation is free of contaminant proteolytic activity and is almost homogenous chromatographically, but it produces a complex pattern under electrophoresis in 30% polyacrylamide gel, which is probably due to enzyme autolysis. As evidenced from the effect of protease A on A and B chains of insulin, the enzyme has a wide substrate specificity. It hydrolyses native vetch legumin and vicilin up to peptides having on average 9 and 16 amino acid residues respectively. No free amino acids were found in hydrolysates of both vetch proteins. Thus, protease A is an endopeptidase, which probably plays the main role in the process of reserve proteins degradation.
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