Tsung P K, Showell H J, Kegeles S W, Becker E L
Biochim Biophys Acta. 1976 Aug 12;445(1):112-7. doi: 10.1016/0005-2744(76)90164-9.
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.
兔腹膜中性粒细胞的趋化活性和N-乙酰-DL-苯丙氨酸β-萘酯酶活性可通过DEAE纤维素柱层析和葡聚糖G-100柱层析彼此分离。从DEAE纤维素层析获得的部分纯化酯酶的分子量为70000。然而，该部分纯化级分含有趋化活性，主要活性分子量为28000，次要活性分子量为45000、21900、14500和10500。酯酶活性可被10⁻⁷M对硝基苯基乙基-5-氯戊基膦酸酯抑制，但趋化活性不受影响。
