title: [Separation of proteolytic enzymes of polymorphonuclear leukocytes of pig peripheral blood].
abstract: Application of gel filtration through Sephadex G-100 (pH 7,5) and ion-exchange chromatography on KM-Sephadex G-50 (pH 7.2) made it possible to detect high-active proteolytic enzymes: elastase-like esterases and serine proteinases in the granular fraction of polymorphonuclear leucocytes of pig peripheral blood. Their pH optimum is for hydrolysis of p-butyltetroxy-L-alanine n-nitrophenyl ester in the weak alkaline medium, for the splitting of histones-in the neutral and weakly alkaline media. Ion-exchange chromatography revealed a sharp increase in the total activity of elastase-like esterase, which may evidence for a separation of the inhibitor at the given stage of the enzyme purification. This is also confirmed by a considerable decrease in the activity of the serine proteinase fraction when adding proteins possessing the activity of elastase-like esterase.
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D010450:Endopeptidases / Q000097:blood; D007700:Kinetics; D009504:Neutrophils / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000097:blood; D010447:Peptide Hydrolases / Q000097:blood* / Q000302:isolation & purification; D012697:Serine Endopeptidases; D013552:Swine
chemical_list: D010450:Endopeptidases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D010196:Pancreatic Elastase
vernacular_title: Razdelenie proteoliticheskikh fermentov polimorfnoiadernykh leĭkotsitov perifericheskoĭ krovi svin'i.