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研究了文昌鱼碱性磷酸酶(AKP)的变性作用,结果表明:低浓度盐酸胍(0.5 mol/l,1.0 mol/l)对该酶具有明显激活作用;酶的荧光构象变化指标随脲浓度增大呈现两个陡变区(1.0～2.0 mol/l,4.0～8.0 mol/l),蜂位因变性剂存在而明显红移,表明肽链己发生较明显的伸展,该酶的失活与变性过程均为一级反应,低浓度脲(2.0 mol/l)作用表现为构象变化略快于失活,而高浓度盐酸胍(2.0 mol/l,4.0 mol/l)及高浓度脲(4.0 mol/l,6.0 mol/l,8.0 mol/l)作用均表现为失活略快于构象变化。
The denaturation of amphioxus alkaline phosphatase (AKP) was studied. The results showed that low concentration of guanidine hydrochloride (0.5 mol / l, 1.0 mol / l) could obviously activate the enzyme. The fluorescence conformation index of the enzyme changed with the concentration of urea (1.0 ~ 2.0 mol / l, 4.0 ~ 8.0 mol / l) showed a red shift remarkably in the presence of a denaturing agent, which indicated that the peptide chain had a more pronounced extension. The inactivation of the enzyme The denaturation process was a first-order reaction. The effect of low concentration of urea (2.0 mol / l) showed a conformational change slightly faster than inactivation, while the high concentration of guanidine hydrochloride (2.0 mol / l, 4.0 mol / mol / l, 6.0 mol / l, 8.0 mol / l) showed inactivation slightly faster than the conformational change.