鸡（家鸡）蛋黄中的氨肽酶Ey对趋化肽的失活作用。
Inactivation of chemotactic peptides by aminopeptidase Ey from hen's (Gallus gallus domesticus) egg yolk.
作者信息
Tanaka T, Ichishima E
机构信息
Research Institute of Q.P. Corp., Tokyo, Japan.
出版信息
Comp Biochem Physiol Biochem Mol Biol. 1994 Apr;107(4):533-8. doi: 10.1016/0305-0491(94)90181-3.
PMID:8205380
Abstract
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.
摘要
对从母鸡（家鸡）蛋黄中纯化得到的氨肽酶Ey针对N-封闭肽的特异性进行了研究。在所测试的肽中，该酶仅水解N-甲酰甲硫氨酰肽。N-甲酰甲硫氨酰-亮氨酰-苯丙氨酸（fMet-Leu-Phe）与氨肽酶Ey孵育后，对人中性粒细胞失去了趋化活性。
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