The activation of lipoprotein lipase by lipase co-protein (apo C-2).
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.
D001053:Apolipoproteins / Q000502:physiology*; D004789:Enzyme Activation; D006801:Humans; D007700:Kinetics; D008053:Lipid Mobilization; D008071:Lipoprotein Lipase / Q000302:isolation & purification / Q000378:metabolism*; D008079:Lipoproteins, VLDL / Q000502:physiology
D001053:Apolipoproteins; D008079:Lipoproteins, VLDL; D008071:Lipoprotein Lipase