Fielding C J, Fielding P E
Expos Annu Biochim Med. 1977;33:165-72.
Kinetic analysis of activation of lipoprotein lipase by apo C-2 indicates that the lipase co-protein increase the rate of lipolysis by adsorption to enzyme at the lipid interface, with formation of a 1:1 molar complex, whose dissociation constant in the presence of triglyceride substrate is about 3 X 10(-13) moles cm-3. Activation by apo C-2, like that by the entire lipoprotein apoprotein moiety (Fielding and Fielding, 1976) is reversible by inorganic salts and the dependence of activation on medium ion-pair activity supports the concept that such inhibition is mediated through a single specific anion-binding site of the lipase co-protein.
载脂蛋白C-2对脂蛋白脂肪酶激活的动力学分析表明，该脂肪酶辅蛋白通过在脂质界面吸附到酶上，以形成1:1摩尔复合物的方式提高脂解速率，在甘油三酯底物存在下其解离常数约为3×10⁻¹³摩尔/厘米³。载脂蛋白C-2的激活，如同整个脂蛋白载脂蛋白部分的激活一样（菲尔丁和菲尔丁，1976年），可被无机盐逆转，激活对介质离子对活性的依赖性支持了这样一种概念，即这种抑制是通过脂肪酶辅蛋白的单个特异性阴离子结合位点介导的。
