Identification of the lipid-binding cyanogen bromide fragment from the cystine-containing high density apolipoprotein, ApoLP-Gln-II

Samuel E. Lux, Kathryn M. John, Sidney Fleischer, Richard L. Jackson, Antonio Gotto

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

ApoLP-Gln-II is one of the major protein constituents of human plasma high density lipoproteins (HDL). This protein and its two CNBr fragments, C-III (carboxyl-terminal) and C-IV (amino-terminal) were tested for ability to bind phosphatidyl choline by the formation of lipid-protein complexes of density 1.063 to 1.210 gm/ml, by changes induced in circular dichroism, and by the inhibition of the reactivation of delipidated mitochondrial β-hydroxybutyric dehydrogenase. In all three of these experimental procedures, C-III but not C-IV retained the ability to bind phosphatidyl choline. These findings suggest that the phospholipid binding site(s) of apoLP-Gln-II may be localized in the carboxyl-terminal portion of the molecule.

Original languageEnglish (US)
Pages (from-to)23-29
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume49
Issue number1
DOIs
StatePublished - Oct 6 1972

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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