Preparation and properties of immobilized lipoprotein lipase.
Purified bovine milk lipoprotein lipase has been covalently attached to CH-Sepharose with water-soluble carbodiimide. The immobilized enzyme retained enzymic activity and was stimulated 7-fold by the addition of human apolipoprotein C-II. Both [3H]heparin and 125I-labeled apolipoprotein C-II bound to the immobilized enzyme; unlabeled heparin and apolipoprotein C-II competed for binding of their respective labeled compounds. Apolipoprotein C-II did not compete for binding of [3H]heparin and vice versa. Human apolipoprotein C-III did not bind to the immobilized enzyme nor did it compete for apolipoprotein C-II binding. We conclude from these studies that both apolipoprotein C-II and heparin interact with immobilized lipoprotein lipase and that they have different binding sites.
D000818:Animals; D053304:Apolipoprotein C-II; D001053:Apolipoproteins / Q000494:pharmacology; D001056:Apolipoproteins C; D002417:Cattle; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005260:Female; D006493:Heparin / Q000494:pharmacology; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000302:isolation & purification / Q000378:metabolism*; D008892:Milk / Q000201:enzymology
D053304:Apolipoprotein C-II; D001053:Apolipoproteins; D001056:Apolipoproteins C; D004800:Enzymes, Immobilized; D006493:Heparin; D008071:Lipoprotein Lipase