These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Immunoenzyme assessment of human apoB-lipoprotein binding to immobilized receptor of low density lipoproteins. 2. Binding of isolated lipoproteins.
    Author: Tsibulsky VP, Yakushkin VV, Preobrazhensky SN.
    Journal: Biochemistry (Mosc); 1997 Jun; 62(6):603-8. PubMed ID: 9284540.
    Abstract:
    The receptor of low density lipoproteins (LDL-receptor) from bovine adrenal cortex membranes was immobilized in standard 96-well polystyrene plates using monoclonal V5-antibodies to the LDL-receptor. The binding of the immobilized LDL-receptor with human low density lipoproteins (LDL) and very low density lipoproteins (VLDL) was determined using peroxidase-labelled antibodies to human apoB. The value of Kd for the interaction of LDL with the immobilized LDL-receptor for 40 samples of LDL was found to be from 5 to 20 micrograms apoB per ml. The immobilized LDL-receptor failed to bind LDL modified by acetylation or malonic dialdehyde, while the binding of non-modified LDL to the immobilized LDL-receptor was inhibited in the presence of EDTA, which is known to be specific for the interaction of LDL with the LDL-receptor. Unlike LDL, VLDL were more variable in the binding to the LDL-receptor. The value of Kd for the interaction of VLDL with the LDL-receptor for 40 samples of VLDL was found to be from 0.5 to 10 micrograms apoB per ml. Thus, the described method is suggested to study the interaction of apoB-containing lipoproteins with the LDL-receptor.
    [Abstract] [Full Text] [Related] [New Search]