摘要
对十二烷基硫酸钠(SDS)、溴化十二烷基三甲铵(DTMB)、辛基苯基聚氧乙烯基醚(TX-100)与肌酸激酶(C.K.)和超氧化物歧化酶(SOD)的相互作用研究表明,SDS和DTMB对C.K.和SOD的活力的影响明显大于TX-100。在浓度较低时,对酶有一定的激活作用,尤其是SDS在0.01~0.1mmol/L时,可提高SOD的活力70%以上。SDS与带相反电荷的蛋白质结合后,可引起蛋白质沉淀。利用表面活性剂分离蛋白质的混合物,可一次达到电泳纯。
The interactions between surfactants, i. e. sodium dodecylsulfate (SDS), dodecyltrimethyl ammonium bromide (DTMB) and octybenzenepolyoxy ethylenol (TX 100), on the one hand, and proteins, i. e. creatine kinase (CK) and superoxide dismutase (SOD) on the other, was studied. The denaturation ability of SDS and DTMB for proteins was much higher than that of TX 100. At lower concentrations, the surfactants increased the activity of the enzymes: in the range of 0.01~0.1 mmol/L, SDS enhanced SOD activity by as much as 70%. Combined with proteins of opposite charge, SDS induced their precipitation. Therefore, pure protein of electrophoretic grade was obtained when protein mixture was treated with surfactants.
出处
《西南农业大学学报(自然科学版)》
CSCD
1999年第4期338-341,共4页
Journal of Southwest Agricultural University
基金
国家自然科学基金