Xu Y Q, Ding Z K
Key Laboratory of Marine Biology, Shangtou University, Guangdong 515063, People's Republic of China.
Biochemistry (Mosc). 2003 Jun;68(6):639-43. doi: 10.1023/a:1024613725561.
Biliverdin reductase was characterized and purified from the liver of Atlantic salmon (Salmo salar) using a novel enzymatic staining method. The properties of the enzyme are quite different from those of mammals. The purified enzyme is a monomeric protein with a molecular weight of approximately 68 kD and an isoelectric point of around 3.8. The enzyme can utilize both NADH and NADPH as coenzyme, but the kinetic properties of the NADH-dependent and the NADPH-dependent enzyme activities are different: K(m) value for biliverdin IXalpha is 0.6 microM in the NADPH system, while it is 6.8 microM in the NADH system. Both enzyme activities are inhibited by excess biliverdin IXalpha, but the NADPH-dependent enzyme activity is far more susceptible. The optimum pH for activity is 5.5 with NADPH and 6.0 with NADH. The optimum reaction temperature is 35 degrees C.
采用一种新型酶促染色方法，从大西洋鲑（Salmo salar）肝脏中对胆绿素还原酶进行了表征和纯化。该酶的性质与哺乳动物的酶有很大不同。纯化后的酶是一种单体蛋白，分子量约为68 kD，等电点约为3.8。该酶可同时利用NADH和NADPH作为辅酶，但依赖NADH和依赖NADPH的酶活性的动力学性质不同：在NADPH系统中，胆绿素IXα的K(m)值为0.6 microM，而在NADH系统中为6.8 microM。两种酶活性均受到过量胆绿素IXα的抑制，但依赖NADPH的酶活性更易受影响。以NADPH为底物时，酶活性的最适pH为5.5，以NADH为底物时为6.0。最适反应温度为35℃。
