Lecithin:cholesterol aeyltransferase activation and lipid binding by synthetic fragments of apolipoprotein c-i

A. K. Soutar, G. F. Sigler, L. C. Smith, Antonio Gotto, J. T. Sparrow

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Peptide fragments of apolipoprotein C-I (apoLP-C-I) have been synthesized by solid phase methodology. After purification, each peptide showed the correct amino acid analysis and was a single band by polyacrylamide gel electrophoresis. In density gradient ultracentrifugation with vesicles of dimyristoyl phosphatidylcholine, peptide fragments 32-57. 24-57, and 17-57 formed stable complexes while 39-57 did not. With mixed vesicles of dimyristoyl phosphatidylcholine-cholesterol 20 μM of the fragments 32-57, 24-5 7 and 17-57 stimulated lecithin:cholesterol aeyltransferase (LC AT) activity 50,60, and 100% respectively, of the value found for apolipoprotein C-I, while fragment 39-57 was inactive. The results indicate that residues 17-57 contain the structural requirements for LCAT activation by apoLP-C-I, and that residues 32 57 represent one of the major phospholipid binding regions of apoLP-C-I.

Original languageEnglish (US)
Pages (from-to)53-58
Number of pages6
JournalScandinavian Journal of Clinical and Laboratory Investigation
Volume38
Issue numbers150
DOIs
StatePublished - Jan 1 1978

Keywords

  • Cholesterol esterification
  • Circular dichroism
  • Density gradient ultracentrifugation
  • Phospholipid protein interaction
  • Synthetic peptides

ASJC Scopus subject areas

  • Clinical Biochemistry

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