title: [An effective single-stage method of obtaining elastase and cathepsin G from human leukocytes].
abstract: A procedure for one-step rapid isolation of highly purified elastase and cathepsin G from human leucocytes including biospecific chromatography on Gordox-Sepharose is described. Electrophoresis in gradient (10-15%) polyacrylamide gel in the presence of sodium dodecyl sulfate revealed three elastase isoforms with molecular masses of 26.3, 27.8 and 28.9 kDa. Cathepsin G produced one protein band with a 27 kDa mobility. The pH optimum for elastase and cathepsin G are 7.0-7.5 and 7.5-8.0, respectively. The specific activities of elastase and cathepsin G preparations as measured by the p-nitrophenyl ester-tert butoxycarbonyl-L-alanine and the ethyl ester-benzoyl tyrosine, hydrolysis are equal to 3-8 and 20-40 mumol/min/mg protein, respectively.
authors.forename: E A
authors.initials: EA
authors.lastname: Neshkova
authors.forename: V L
authors.initials: VL
authors.lastname: Dotsenko
authors.forename: N I
authors.initials: NI
authors.lastname: Larionova
authors.forename: G A
authors.initials: GA
authors.lastname: Iarovaia
mesh_terms: D056649:Cathepsin G; D002403:Cathepsins / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D019272:Leukocyte Elastase; D007962:Leukocytes / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000302:isolation & purification*; D012697:Serine Endopeptidases
chemical_list: D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase
vernacular_title: Effektivnyĭ odnoétapnyĭ metod polucheniia élastazy i katepsina G izleĭkotsitov cheloveka.