A simple method for purification of chymase from rat tongue and rat peritoneal cells.
Chymase was purified from rat tongue and rat peritoneal cells by a simple new method involving hydrophobic chromatography on octyl-Sepharose 4B and hydroxylapatite column chromatography. This procedure can be completed in 1 or 2 days and the recovery is 45-60% from rat tongue and 32-47% from rat peritoneal cells. The specific activity of the purified enzyme is higher than that of crystallized enzyme previously reported (Y. Sanada, N. Yasogawa, and N. Katunuma (1978) Biochem. Biophys. Res. Commun. 82, 108-113). This procedure should be particularly useful for purifying chymase on a large scale from tissues in which it is present in relatively low concentrations.
D000818:Animals; D001202:Ascitic Fluid; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D012085:Chymosin / Q000302:isolation & purification*; D005779:Immunodiffusion; D008297:Male; D008407:Mast Cells / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D014059:Tongue / Q000201:enzymology*
D012085:Chymosin