Inactivation of chemotactic peptides by aminopeptidase Ey from hen's (Gallus gallus domesticus) egg yolk.
Aminopeptidase Ey, purified from hen's (Gallus gallus domesticus) egg yolk, was studied for its specificity against N-blocked peptides. Only N-formylmethionyl peptides were hydrolyzed by the enzyme in the tested peptides. N-Formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) lost its chemotactic activity toward human neutrophil after incubation with aminopeptidase Ey.
Tanaka
T
T
Research Institute of Q.P. Corp., Tokyo, Japan.
Ichishima
E
E
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D030161:Avian Proteins; D002630:Chemotactic Factors / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D002634:Chemotaxis, Leukocyte / Q000187:drug effects; D002645:Chickens; D005260:Female; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D008969:Molecular Sequence Data; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D009504:Neutrophils / Q000502:physiology; D009842:Oligopeptides / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D010063:Ovum / Q000201:enzymology; D013379:Substrate Specificity
D030161:Avian Proteins; D002630:Chemotactic Factors; D009842:Oligopeptides; D009240:N-Formylmethionine Leucyl-Phenylalanine; D000626:Aminopeptidases; C085350:aminopeptidase Ey, Gallus gallus