The binding of low density lipoprotein by liver membranes in the pig

P. S. Bachorik, J. N. Livingston, J. Cooke, P. O. Kwiterovich

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Porcine liver membranes are capable of high affinity binding of homologous low density lipoproteins (LDL). Binding is time and temperature dependant and substrate saturable. High affinity binding sites are half saturated at 11 μg/ml lipoprotein-protein. The binding of 125I-LDL is inhibited by unlabelled homologous LDL, very low density lipoproteins (VLDL) and high density lipoproteins (HDL) and also be human LDL and HDL, but not by unrelated proteins tested. The binding and displacement patterns with membranes from several other porcine tissues are similar to those of liver membranes. These results suggest the presence of "lipoprotein binding sites" in liver membranes which recognize structural features common to the lipoproteins and further indicate that liver membranes are not unique in their ability to bind LDL.

Original languageEnglish (US)
Pages (from-to)927-935
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Apr 19 1976
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'The binding of low density lipoprotein by liver membranes in the pig'. Together they form a unique fingerprint.

Cite this