Dzugaj A, Gancarz R
Department of Animal Physiology, University of Wrocław, Poland.
Acta Biochim Pol. 1990;37(4):433-44.
The interaction of D-fructose-1,6-bisphosphate 1-phosphohydrolase (Fru-P2-ase, EC 3.1.3.11), with bovine serum albumin (BSA) results in the fluorescence quenching of BSA. BSA increases fluorescence anisotropy of Fru-P2-ase modified with o-phthaldialdehyde. A program in Fortran, to simulate the experimental titration curves of BSA with Fru-P2-ase and o-phthaldialdehyde modified Fru-P2-ase with BSA, was written. For fluorescence quenching experiments the best fit was obtained for a model where one subunit of native Fru-P2-ase binds up two molecules of BSA. The determined dissociation constants at 5, 15, 25 and 35 degrees C were 2.2, 1.6, 0.83 and 0.03 microM, respectively.
1,6 - 二磷酸 - D - 果糖1 - 磷酸水解酶（Fru - P2 - 酶，EC 3.1.3.11）与牛血清白蛋白（BSA）相互作用会导致BSA的荧光猝灭。BSA会增加经邻苯二甲醛修饰的Fru - P2 - 酶的荧光偏振度。编写了一个Fortran程序来模拟用Fru - P2 - 酶滴定BSA以及用经邻苯二甲醛修饰的Fru - P2 - 酶滴定BSA的实验滴定曲线。对于荧光猝灭实验，天然Fru - P2 - 酶的一个亚基结合两分子BSA的模型能得到最佳拟合。在5、15、25和35摄氏度下测定的解离常数分别为2.2、1.6、0.83和0.03微摩尔。
