Tsung P, Kegeles S W, Showell H J, Becker E L
Biochim Biophys Acta. 1975 Sep 22;403(1):98-105. doi: 10.1016/0005-2744(75)90012-1.
An N-acetyl-DL-phenylalanine beta-naphthyl esterase has been purified 26-fold from rabbit peritoneal polymorphonuclear leukocytes. The purified enzyme was inhibited by 10(-7) M p-nitrophenylethyl-5-chloropentylphosphonate. The apparent Km for hydrolysis of N-acetyl-DL-phenylalanine beta-naphthyl ester is 71 muM. Optimal reaction rates were observed at pH 6-8. No divalent cation requirement for the activation of the enzyme activity was observed. The esterase activity was neither inhibited nor stimulated by bacterial factor, complement component C5a, guanosine 3',5'-monophosphate (cyclic GMP) and adenosine 3',5'-monophosphate (cyclic AMP) which are attractants or repellents for polymorphonuclear leukocytes. High chemotactic activity was observed in the partially purified fraction of the enzyme. The chemotactic activity, like the enzyme activity, was completely inhibited by 10(-7) M phosphonate.
已从兔腹膜多形核白细胞中纯化出一种N-乙酰-DL-苯丙氨酸β-萘酯酶，纯化倍数为26倍。纯化后的酶被10⁻⁷M对硝基苯乙基-5-氯戊基膦酸酯抑制。N-乙酰-DL-苯丙氨酸β-萘酯水解的表观Km为71μM。在pH 6 - 8时观察到最佳反应速率。未观察到酶活性激活需要二价阳离子。酯酶活性既不受细菌因子、补体成分C5a、鸟苷3',5'-单磷酸（环鸟苷酸）和腺苷3',5'-单磷酸（环腺苷酸）的抑制，也不受其刺激，这些物质对多形核白细胞来说是趋化剂或驱化剂。在该酶的部分纯化级分中观察到高趋化活性。与酶活性一样，趋化活性被10⁻⁷M膦酸酯完全抑制。
