Apolipoprotein E-mediated binding of hypertriglyceridemic very low density lipoproteins to isolated low density lipoprotein receptors detected by ligand blotting Academic Article Article uri icon


MeSH Major

  • Obesity
  • Thinness
  • Weight Gain


  • HTG-VLDL1, like LDL, bind with high affinity to electrophoretically transferred, isolated LDL receptors partially purified from bovine adrenal glands. Ligand blotting techniques show that binding is calcium dependent; little or no binding of LDL or HTG-VLDL1 is observed in the presence of 10 mM EDTA. HTG-VLDL1 does not bind in the presence of 7 mM suramin, an inhibitor of LDL binding to the LDL receptor. Pretreatment of LDL with either thrombin or trypsin does not affect apoB-mediated LDL binding to the LDL receptor. ApoE-mediated binding of HTG-VLDL1 to the blotted LDL receptor is abolished or greatly decreased by thrombin treatment of HTG-VLDL1; trypsin treatment of HTG-VLDL1 abolishes binding. Reincorporation of apoE into trypsinized HTG-VLDL1 restores binding. These studies demonstrate unequivocally that HTG-VLDL1 bind to the LDL receptor, that the binding of HTG-VLDL1 to the isolated LDL receptor is mediated through the thrombin-accessible apoE, and that HTG-VLDL1 which bind via potentially dissociable apoE rather than non-transferable apoB can be used for ligand blotting.

publication date

  • August 29, 1986



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/S0006-291X(86)80118-8

PubMed ID

  • 3094511

Additional Document Info

start page

  • 333

end page

  • 40


  • 139


  • 1