Activation of lipoprotein lipase by N-α-palmitoyl (56–79) fragment of apolipoprotein C-II
| Autor: | Ann E. Rechtin, Richard L. Jackson, Larry R. McLean, Rudy A. Demel, Ambikaipakan Balasubramaniam |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
Apolipoprotein B
Apolipoprotein C-II Palmitates Biophysics Peptide Biochemistry Acylation Structure-Activity Relationship chemistry.chemical_compound Phosphatidylcholine Humans Apolipoproteins C Molecular Biology chemistry.chemical_classification Lipoprotein lipase biology Vesicle Cell Biology Lipid Metabolism Peptide Fragments Enzyme Activation Lipoprotein Lipase chemistry Dipalmitoylphosphatidylcholine biology.protein lipids (amino acids peptides and proteins) |
| Zdroj: | Biochemical and Biophysical Research Communications. 137:1041-1048 |
| ISSN: | 0006-291X |
| Popis: | The effect of apolipoprotein C-II (apoC-II) and a synthetic fragment of apoC-II corresponding to residues 56-79 on the lipoprotein lipase (LpL) catalyzed hydrolysis of trioleoylglycerol in a monolayer of egg phosphatidylcholine and of dipalmitoylphosphatidylcholine vesicles was examined. Synthetic peptide 56-79, which does not associate with lipid, did not activate LpL at surface pressures greater than 30 mN/m; apoC-II is active up to 34 mN/m. However, acylation of the NH2-terminus of peptide 56-79 with palmitoyl chloride gave nearly identical LpL activating properties as compared to apoC-II. We conclude that at high surface pressures the lipid-binding region of apoC-II (residues 44-55) plays an essential role in LpL activation. |
| Databáze: | OpenAIRE |
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