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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.
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
October 1986,
Biochimica et biophysica acta,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
January 1980,
Annals of the New York Academy of Sciences,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
April 1983,
Biochemistry,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
June 1979,
Biochimica et biophysica acta,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
October 1987,
Chemistry and physics of lipids,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
January 1982,
La Ricerca in clinica e in laboratorio,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
March 1990,
The Journal of biological chemistry,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
June 1987,
Biochemistry,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
May 1983,
The Journal of biological chemistry,
A Balasubramaniam, and
A Rechtin, and
L R McLean, and
R L Jackson, and
R A Demel
January 1982,
Biophysical journal,
