中文摘要：

通过匀浆、硫酸铵沉淀、SephadexG-100凝胶过滤和Phenyl—SepharoseHP疏水层析，从猪后腿肉中分离纯化了一种亮氨酰氨肽酶，并对其部分生化特性进行了研究。结果表明：亮氨酰氨肽酶的得率为12．14％，纯化了77．62倍；亮氨酰氨肽酶的最适温度为40℃左右，最适pH为7．0左右，Mg2＋对酶活性有激活作用，Zn2＋、Cu2＋、Co2＋、EDTA和EGTA对酶活性有抑制作用；Ca2＋、Fe2＋和Mn2＋对亮氨酰氨肽酶活性的影响取决于离子浓度，浓度为0．5mmol·L^-1时对酶具有激活作用，而浓度为1．0mmol·L^-1时则表现为抑制作用。

英文摘要：

A kind of leucyl aminopeptidase was isolated and purified from pig hind legs by using homogenation, ammonium sulfate precipitation, Sephadex G-100 gel filtration and Phenyl-Sepharose HP hydrophobic chromatography, of which some biochemical char- acteristics were investigated. The results showed the purification fold and yield were 77. 62 and 12. 14% , respectively. The aminopeptidase activity was optimal at 40 ℃ and pH 7.0, stimulated by Mg2＋ ions and inhibited by Zn2＋, Cu2＋ , Co2＋ ions and EDTA, EGTA. The effects of Ca2＋, Fe2＋ and Mn2＋ on enzyme activity depended on their different concentrations, which could improve the enzyme activity at the concentration of 0.5 mmol. L^-1 and inhibit at the concentration of 1.0 mmol· L^-1.