Chemotactic activity from rabbit peritoneal neutrophils. Lack of identity with N-acetyl-DL-phenylalanine beta-napthyl esterase.
The chemotactic and N-acetyl-DL-phenylalanine beta-naphthyl esterase activities of rabbit peritoneal neutrophils are separable from each other by both DEAE cellulose and Sephadex G-100 column chromatography. Partially purified esterase obtained from DEAE-cellulose chromatography had molecular weight of 70 000. However, the partially purified fraction contained chemotactic activities with major activity in molecular weight of 28000 and minor activities in the molecular weights of 45000, 21900, 14500 and 10500. Esterase activity is inhibited by 10(-7) M p-nitrophenylethyl-5-chloropentylphosphonate but chemotactic activity is not.
D000626:Aminopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001202:Ascitic Fluid / Q000201:enzymology*; D002633:Chemotaxis; D008970:Molecular Weight; D009504:Neutrophils / Q000201:enzymology*; D009578:Nitrobenzenes / Q000494:pharmacology; D009943:Organophosphorus Compounds / Q000494:pharmacology; D011817:Rabbits
D009578:Nitrobenzenes; D009943:Organophosphorus Compounds; D000626:Aminopeptidases