[An effective single-stage method of obtaining elastase and cathepsin G from human leukocytes]

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.