在胍溶液中文昌鱼酸性磷酸酶活性部位的构象变化与活力变化的关系

Activity and Conformational Changes at the Active Site ofACPase from Branchiostoma belcheri (Gray) in Guanidine Solutions

盐酸胍中酸性磷酸酶活性部位构象变化与活力变化的关系，酶于０．６ｍｏｌ／ＬＧｕ－ＨＣｌ中，其相对活力提高２０％，当ＧＵ－ＨＣｌ浓度增加到１．２～２．４ｍｏｌ／Ｌ时，酶的相对活力，其活性部位紫外－可见光谱５００ｍｍ处吸收峰及荧光发射光谱５１５ｍｍ处的发射峰值下降，同时测定了酶的变性与失活常数。

Activity and conformational changes at the active site of ACPase in the presence of different concentration of Gu HCl have been studied by using fluorescence emission spectroscopy With 0.6 mol/L Gu HCl,the enzyme relative activity was increased by 20%.As Gu HCl concentration increases from 1.2 to 2.4 mol/L,the enzyme relative activity and the intensity in the fluorescence emission peak at 515 nm were reduced .The constants of denaturation and inactivation of ACPase in Gu HCl have also been determined .Result indicates that the rate constant of denaturetion is greater than those of inactivation .The relationship between the reactivation and the refolding of the enzyme has been investigated.