title: Monoclonal antibodies against bovine milk lipoprotein lipase. Characterization of an antibody specific for the apolipoprotein C-II binding site.
abstract: Ten murine monoclonal antibodies have been produced that are specific for bovine milk lipoprotein lipase. One monoclonal antibody, bLPL-mAb-7, inhibited completely the apolipoprotein C-II (apo-C-II)-dependent enzymic hydrolysis of trioleoylglycerol in a phospholipid-stabilized emulsion, but had no effect on the hydrolysis of the water-soluble substrate p-nitro-phenylacetate. Four times more bLPL-mAb-7 was required to achieve 50% inactivation of lipoprotein lipase activity when the enzyme was preincubated with excess apo-C-II. Disruption of the binding of a dansyl-labeled apo-C-II peptide to lipoprotein lipase by bLPL-mAb-7 was demonstrated by resonance energy transfer, both in the presence and absence of lipid. This antibody thus appears to recognize the apo-C-II binding site of lipoprotein lipase. In addition, bLPL-mAb-7 also inhibited the lipoprotein lipase activity of human post-heparin plasma.
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D053304:Apolipoprotein C-II; D001056:Apolipoproteins C / Q000378:metabolism*; D001665:Binding Sites; D004735:Energy Transfer; D006493:Heparin; D006868:Hydrolysis; D008071:Lipoprotein Lipase / Q000276:immunology* / Q000378:metabolism; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008892:Milk / Q000201:enzymology*; D009596:Nitrophenols / Q000378:metabolism; D014280:Triglycerides / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D053304:Apolipoprotein C-II; D001056:Apolipoproteins C; D009596:Nitrophenols; D014280:Triglycerides; C008642:4-nitrophenyl acetate; D006493:Heparin; D008071:Lipoprotein Lipase