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.$$$$
出处
《南开大学学报（自然科学版）》
CAS
CSCD
北大核心
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)
关键词
L-半胱氨酸脱巯基酶
假单胞菌
酶纯化
酶性质
L-cysteine desulfhydrases
Pseudomonas sp.
purification of enzyme
properties of enzyme
