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


MeSH Major

  • Obesity
  • Thinness
  • Weight Gain


  • 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. © 1972.

publication date

  • October 6, 1972



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/0006-291X(72)90004-6

PubMed ID

  • 4342724

Additional Document Info

start page

  • 23

end page

  • 9


  • 49


  • 1