假单胞菌TS-1138 L-半胱氨酸脱巯基酶的纯化和性质研究  

PURIFICATION AND THE PROPERTIES OF L-CYSTEINE DESULFHYDRASE PSEUDOMONAS SP.TS1138

作　　者：金永杰[1] 杨文博[1] 刘忠[1] 白钢[1] 孙丹[1] 

机构地区：[1]南开大学生命科学学院,天津300071

出　　处：《南开大学学报（自然科学版）》2004年第4期100-104,共5页Acta Scientiarum Naturalium Universitatis Nankaiensis

基　　金：国家自然科学基金资助项目(30470053)

摘　　要：假单胞菌TS-1138L-半胱氨酸脱巯基酶经DEAECellulose-52阶段洗脱、SephadexG-100柱层析被纯化了80.3倍,SDS-PAGE鉴定为单一条带,该酶的相对分子质量为53.0kDa;酶反应的最适pH为7.5,最适反应温度为35℃,该酶的米氏常数为2.37μmol/L,最大反应速度为0.11μmol/mL·min·Pb2+对该酶有很强的激活作用,Zn2+对该酶有较强的抑制作用,羟胺为该酶特异性的抑制剂.The L-cysteine desulfhydrase from Pseudomonas sp. TS-1138 is purified about 80.3 fold by phase elution of DEAE cellulose-52 and gel filtration of Sephadex G-100. The purified enzyeme is demonstrated by SDS-PAGE to be a homogeneous protein. Its molecular weight is about 53.0 kDa. The optimum conditions are pH 7.5 and 35 ℃ respectiviely. The Km and Vmax of the enzyme are 2.37 μmol/L and 0.11 μmol/mL·min respectively. Pb^2+ enhance the enzyme activity sharply, whereas Zn^2+ inhibit the enzyme actvity significantly. Hydroxylamine is a special inhibitor of the enzyme.$$$$

关 键 词：L-半胱氨酸脱巯基酶 假单胞菌 酶纯化 酶性质 

分 类 号：Q814.1[生物学—生物工程]