Application of poly-L-lysine to purification of leukocyte cathepsin G by affinity chromatography.
Poly-L-lysine with molecular masses of 3.3-290 kDa increased the amidolytic activities of leukocyte elastase and cathepsin G at low concentration, but had little effect on the activities of pancreatic elastase, alpha-chymotrypsin, plasmin and thrombin. Highly purified cathepsin G was obtained from column of EAH Sepharose 4B or Suc-L-Tyr-D-Leu-D-Val-pNA-Sepharose (affinity chromatography) by elution with poly-L-lysine solution (0.4 mg/ml, molecular weight (MW.) 290000 or 2.2 mg/ml, MW. 3300). Leukocyte elastase, adsorbed to Suc-L-Tyr-D-Leu-D-Val-pNA-Sepharose, was not eluted with poly-L-lysine solution. The amino acid composition of purified cathepsin G has been determined.
Nagamatsu
Y
Y
Faculty of Nutrition, Kobe-Gakuin University, Japan.
Yamamoto
J
J
Kanamoto
A
A
Tsuda
Y
Y
Okada
Y
Y
D000595:Amino Acid Sequence; D056649:Cathepsin G; D002403:Cathepsins / Q000097:blood / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D006801:Humans; D066298:In Vitro Techniques; D007962:Leukocytes / Q000737:chemistry*; D008969:Molecular Sequence Data; D011107:Polylysine / Q000494:pharmacology*; D012697:Serine Endopeptidases
D011107:Polylysine; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G