Abnormal interaction of the human apolipoprotein A-I variant [Lys107→0] with high density lipoproteins Academic Article Article uri icon


MeSH Major

  • Obesity
  • Thinness
  • Weight Gain


  • Several isoforms of apoprotein A-I [apoA-I], the major apoprotein of high density lipoproteins [HDL], have been described. We compared the in vivo and in vitro properties of normal human apoA-I with those of apoA-I [Lys107----0]. Fluorescence and circular dichroic spectra showed that deletion of Lys107 decreases apoprotein self-association. In vivo metabolic studies in the rat indicated that the interaction of apoA-I [Lys107----0] with HDL was lower than normal. We conclude that deletion of Lys107 results in a reorganization of the apoprotein structure that decreases its potential to form hydrophobic associations.

publication date

  • December 31, 1985



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/0006-291X(85)91213-6

PubMed ID

  • 3936504

Additional Document Info

start page

  • 856

end page

  • 62


  • 133


  • 3