Isolation of a helical, lipid-binding fragment from the human plasma high density lipoprotein, apolp-GLN-I

R. L. Jackson, H. N. Baker, J. S.K. David, Antonio Gotto

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

The major apolipoprotein of human plasma high density lipoproteins (HDL), apoLP-Gln-I, has previously been shown to have a high content of α-helical conformation and a molecular weight of approximately 28,000. Our results show that apoLP-Gln-I contains three methionine residues. We have treated apoLP-Gln-I with cyanogen bromide (CNBr) and have isolated the four CNBr fragments by chromatography on BioGel P-30. One of the fragments, CNBr-I has 92 amino acid residues, contains no homoserine or methionine and corresponds to the carboxyl-terminal peptide. This fragment is of particular interest since it was shown to retain a high content of α-helix, while the other fragments were mainly disordered, and to possess the ability to bind phosphatidyl choline.

Original languageEnglish (US)
Pages (from-to)1444-1451
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume49
Issue number6
DOIs
StatePublished - Dec 18 1972

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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