PMID: 9554982May 23, 1998Paper

A peptide from hog plasma that inhibits human cholesteryl ester transfer protein

Biochimica Et Biophysica Acta
K H ChoY B Park

Abstract

A peptide that inhibits the human cholesteryl ester transfer protein (CETP) was isolated from hog plasma by ultracentrifugation, two sequential column chromatographies and electroelution from gels. Molecular weight of the peptide was determined to be approximately 3 kDa on the SDS-PAGE. The peptide contained 28 amino acids with an identical sequence to the amino terminus of hog apolipoprotein-CIII except two amino acid residues: -Pro-Glu- at the fifth and sixth amino acids from the amino terminus in the isolated peptide, in contrast to -Leu-Leu- in hog apo-CIII. A peptide synthesized chemically according to the amino acid sequence of the peptide (designated P28) showed approximately the same degree of CETP inhibitory activity as the isolated peptide. Synthetic peptides with different number of amino acids were also tested for CETP inhibition. Among the peptides, the one with 20 amino acid residues (P20) from the amino terminus showed the highest inhibitory activity against the CETP. The peptide appeared to be associated with the hog high-density lipoproteins (HDL), as determined by immunoblot analysis using antibody against P28. The CETP-inhibitory activity of the peptide was examined in vivo using diet-induced hypercholesterol...Continue Reading

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Citations

May 24, 2003·Clinica Chimica Acta; International Journal of Clinical Chemistry·Myung-Ja KwonYeong-Ok Song
Aug 10, 2000·Drugs·P H Chong, B S Bachenheimer
Mar 22, 2007·European Journal of Clinical Investigation·S H ParkK H Cho
Nov 13, 2004·Canadian Journal of Applied Physiology = Revue Canadienne De Physiologie Appliquée·James R Turk, M Harold Laughlin

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