A monoclonal antibody against human lipoprotein lipase inhibiting heparin binding without affecting catalytic activity
| Autor: | M R Ven Murthy, François Cadelis, Yves Deshaies, Pierre Julien, J P Valet, Paul-J. Lupien |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
medicine.drug_class
Enzyme-Linked Immunosorbent Assay Biology Monoclonal antibody Biochemistry Epitope Antigen medicine Humans Binding site Molecular Biology Lipoprotein lipase Expression vector Binding Sites Heparin Myocardium digestive oral and skin physiology nutritional and metabolic diseases Antibodies Monoclonal Cell Biology Molecular biology Molecular Weight Lipoprotein Lipase Adipose Tissue biology.protein lipids (amino acids peptides and proteins) Electrophoresis Polyacrylamide Gel Antibody medicine.drug |
| Zdroj: | Biochemistry and cell biology = Biochimie et biologie cellulaire. 74(3) |
| ISSN: | 0829-8211 |
| Popis: | A fragment of the human lipoprotein lipase (LPL) cDNA (405 bp, 5′ terminal end) was cloned in an expression vector to produce a ~17 kDa fusion peptide and was used as antigen to produce a high titre anti-LPL monoclonal antibody (10C3 MAb). This antibody reacts with both native and denatured forms of LPL from different tissue and animal sources. Competition studies with heparin indicate that 10C3 MAb is specific for an epitope at a heparin binding site. The antibody does not inhibit LPL enzyme activity, indicating that the antigenic epitope is not situated within or in the proximity of the LPL catalytic region. With these characteristics, 10C3 MAb should prove to be a useful immunochemical tool in clinical as well as in fundamental investigations on the metabolism of triglyceride-rich lipoproteins and in studies on the functional anatomy of LPL.Key words: lipoprotein lipase, monoclonal antibody, LPL cDNA, heparin, immunoassay, ELISA. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|