Rathelot J, Julien R, Bosc-Bierne I, Gargouri Y, Canioni P, Sarda L
Biochimie. 1981 Mar;63(3):227-34. doi: 10.1016/s0300-9084(81)80196-4.
Horse pancreatic lipase has been purified from tissue homogenates. Molecular and catalytic properties of horse lipase are comparable to those of the pancreatic lipases previously isolated. Kinetic studies of the inhibition of horse lipase activity by bile salts and of reactivation by pure colipase from three species (horse, ox and pig) allowed to calculate the apparent dissociation constant (Kd) of the lipase-colipase complex in the presence of the substrate (triolein). Identical values of Kd were found in all three cases (Kd = 1.1 10(-9) M). These values are lower by several orders of magnitude than that published for the binding between lipase and colipase in the absence of substrate. Qualitative experiments show that the activation of horse lipase can be accomplished by rat, dog and chicken colipase as well. The interaction between lipase and colipase is enhanced when the complex is adsorbed at the lipid-water interface. This specific protein-protein interaction is preserved in heterologous mixtures using colipases from other animal species.
马胰脂肪酶已从组织匀浆中纯化出来。马脂肪酶的分子和催化特性与先前分离出的胰脂肪酶相当。对胆盐抑制马脂肪酶活性以及三种动物（马、牛和猪）的纯辅脂酶使其重新激活进行动力学研究，从而得以计算在底物（三油酸甘油酯）存在下脂肪酶 - 辅脂酶复合物表观解离常数（Kd）。在所有三种情况下均发现相同的Kd值（Kd = 1.1×10⁻⁹ M）。这些值比在无底物情况下脂肪酶与辅脂酶结合所公布的值低几个数量级。定性实验表明，大鼠、狗和鸡的辅脂酶也能激活马脂肪酶。当复合物吸附在脂质 - 水界面时，脂肪酶与辅脂酶之间的相互作用会增强。在使用其他动物物种的辅脂酶的异源混合物中，这种特定的蛋白质 - 蛋白质相互作用得以保留。
