On the pH dependency of lipoprotein lipase activity.
The relation between pH and activity for lipoprotein lipase against emulsions of long-chain triacylglycerols has previously been studied in several laboratories and found to be a bell-shaped curve with optimum activity between pH 8 and 9. In contrast, using short-chain triacylglycerols or monoacylglycerols as substrates we had found that the activity rises continuously with pH to at least pH 10.5. This suggested that some factor other than the active site mechanism limited the activity at high pH in traditional assay systems. We, therefore, reinvestigated the activity against long-chain triacylglycerols under conditions where binding of the enzyme to the emulsion droplets and enzyme stability was not limiting. Under these conditions the activity continued to rise from pH 8 to pH 10, and the degree of stimulation by apolipoprotein C-II was found to be the same over the whole range studied (pH 6.5-10.5).
D000818:Animals; D053304:Apolipoprotein C-II; D001053:Apolipoproteins / Q000494:pharmacology; D001056:Apolipoproteins C; D002417:Cattle; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008892:Milk / Q000201:enzymology
D053304:Apolipoprotein C-II; D001053:Apolipoproteins; D001056:Apolipoproteins C; D008071:Lipoprotein Lipase