CAJ | 학술논문

用分子生物学方法表达、纯化了游仆虫中心蛋白及N-端半分子,用铽荧光探针法、离子竞争法研究了pH 7.4,0.01 mol·L-Hepes条件下中心蛋白与铽、钙的结合性质.结果表明中心蛋白有4个铽结合部位,其中2个为高亲合结合部位、2个为低亲合结合部位.具有2个低亲合结合部位的中心蛋白半分子与铽结合的条件常数是(2.13±0.10)×10 5 L·mol-1,与钙结合的条件常数是(7.52±0.02)×102L·mol-1.
용분자생물학방법표체、순화료유부충중심단백급N-단반분자,용특형광탐침법、리자경쟁법연구료pH 7.4,0.01 mol·L-Hepes조건하중심단백여특、개적결합성질.결과표명중심단백유4개특결합부위,기중2개위고친합결합부위、2개위저친합결합부위.구유2개저친합결합부위적중심단백반분자여특결합적조건상수시(2.13±0.10)×10 5 L·mol-1,여개결합적조건상수시(7.52±0.02)×102L·mol-1.
Euplotes centrins (EoCens) including full-length protein (apoEoCen) and semi-molecule centrin (NapoEoCen) were expressed and purified by biological engineering. The binding of terbium (Tb3+) to apoEoCen was 7.4. It could be seen that the protein binds two Tb3+ with high affinity and two Tb3+ with low affinity. The reac tions between N-apoEoCen and Tb3+ or Ca2+ were also studied by Tb3+ fluorescence probe and ionic competition in