乙醇对文昌鱼酸性磷酸酶活力与构象的影响

文昌鱼酸性磷酸酶是一种含有铁离子的金属酶，酶的紫外－可见光谱扫描，２８０ｎｍ，５００ｎｍ有最大吸收峰，３２０ｎｍ有肩峰。荧光扫描：在２８１ｎｍ激发下，３３０ｎｍ有发射峰，在４８０ｎｍ激发下，５１５ｎｍ有一发射峰。

Changes of conformation and activity of ACPase from Branchoistoma belcheri in ethanol solutions

The previous studies by our research team have shown that Branchiostoma belcheri Acid Phosphatase (ACPase, E. C. 3. 1. 3. 2) was a kind of metalloenzyme which exhibits an absorption peak with the warelength at 500nm in its visible spectra and an emission peak with the warelength at 515nm in its fluorescence spectra because its containing iron. This two charactal peaks are sensitive to the enzyme activity (referance 7~9 for detail). Changes of conformation and activity at the active site of the ACPase in different eoncentration(V/V) of ethanol solutions has been investigated by means of fiuorescence emission and UV-visible spectra. Kinetic analysis of the inhibition shows that the inhibition of ethanol on the enzyme is found to be of uncompetitive type and the inhibition constants is found to be 16%. The rate constants of denaturation are faster than those of inactivation in the presence of ethanol.