title: [Partial purification and characterization of protease A of germinating vetch seeds, hydrolyzing native reserve proteins].
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.
mesh_terms: D007887:Fabaceae / Q000201:enzymology* / Q000254:growth & development; D007328:Insulin / Q000378:metabolism; D010446:Peptide Fragments; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D010940:Plant Proteins / Q000378:metabolism; D010946:Plants, Medicinal; D012639:Seeds / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D007328:Insulin; D010446:Peptide Fragments; D010940:Plant Proteins; D010447:Peptide Hydrolases
vernacular_title: Chastichnaia ochistka i kharakteristika proteazy A prorostaiushchikh semian viki, gidrolizuiushcheĭ nativnye zapasnye belki.