The evidence for the existence of chymotrypsin-like esterase activity in the plasma membranes of rabbit neutrophils and the specific chemotactic peptide binding activity of the subcellular fractions.
1. Light- and heavy-plasma membrane fractions have been isolated from rabbit neutrophils and a chymotrypsin-like esterase has been shown to be present in these fractions. 2. The molecular weight of the chymotrypsin-like esterase of rabbit neutrophil plasma membrane was estimated to be about 200 000. 3. About 93% of the chymotrypsin-like esterase of the plasma membranes is esterase 1 and the susceptibility to potential inhibitors was similar in light- and heavy-plasma membrane. 4. Chemotactic peptide, [3H]formyl-norleucyl-leucyl-phenylalanine [3H]formyl-Nle-Leu-Phe) binding by subcellular fractions shows that the highest specific binding was observed in the light-plasma membrane was about 2-fold higher than the heavy-plasma membrane, about 37-fold higher than the nuclear fraction, about 3-fold higher than lysosomal fraction and about 10-fold higher than the microsomal fraction.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002467:Cell Nucleus / Q000201:enzymology; D002634:Chemotaxis, Leukocyte; D002918:Chymotrypsin; D010450:Endopeptidases / Q000302:isolation & purification*; D004950:Esterases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D066298:In Vitro Techniques; D008247:Lysosomes / Q000201:enzymology; D008861:Microsomes / Q000201:enzymology; D008970:Molecular Weight; D009504:Neutrophils / Q000201:enzymology*; D010455:Peptides / Q000378:metabolism; D011817:Rabbits
D010455:Peptides; D004950:Esterases; D010450:Endopeptidases; D002918:Chymotrypsin