Isolation of apolipoprotein-free lipoprotein lipase from human post-heparin plasma
| Autor: | Reagan H. Bradford, Devaki Ganesan |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
Calcium Phosphates
Glycerol Immunodiffusion Apolipoprotein B Polyacrylamide Biophysics Oleic Acids Biochemistry chemistry.chemical_compound Animals Humans Post heparin plasma Immunoelectrophoresis Molecular Biology Triglycerides chemistry.chemical_classification Carbon Isotopes Enzyme Precursors Lipoprotein lipase Sheep biology Heparin Activator (genetics) Goats Immune Sera Fasting Cell Biology Single band Electrophoresis Disc Molecular biology Enzyme Activation Butyrates Lipoprotein Lipase Electrophoresis Enzyme chemistry Injections Intravenous Phosphatidylcholines biology.protein Rabbits Peptides Gels Ultracentrifugation |
| Zdroj: | Biochemical and Biophysical Research Communications. 43:544-549 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(71)90648-6 |
| Popis: | Lipoprotein lipase from human post-heparin plasma was purified at least 10,000-fold using the Fielding procedure. When the purified lipoprotein lipase was subjected to polyacrylamide electrophoresis, a single band with lipolytic activity and four additional bands were observed. These four bands are identical in their electrophoretic and immunochemical properties to the polypeptides of apolipoprotein C. Evidence is presented which suggests that one or more of these polypeptides may serve as a partial activator of this enzyme. |
| Databáze: | OpenAIRE |
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