title: Binding of LPS and LPS--LDL complexes to rat hepatocytes.
abstract: We studied binding of 3H-LPS toxin and LPS complexes with serum 125I-LDL to primary culture of rat hepatocytes. Receptor binding of LPS and LDL--LPS complex was 50 and 77% of the total, respectively. Scatchard plot was linear in both cases. LDL and LDL--LPS complexes were inessential for LPS binding, while LDL--LPS binding was appreciably suppressed by LPS (-30%) and LDL (-65%).
authors: Laboratory of Molecular Mechanisms of Infections, Central Institute of Epidemiology, Moscow. farm@newtech.ru
authors: A V
authors: AV
authors: Viktorov
authors: V A
authors: VA
authors: Yurkiv
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D022781:Hepatocytes / Q000378:metabolism*; D006801:Humans; D008070:Lipopolysaccharides / Q000378:metabolism*; D008077:Lipoproteins, LDL / Q000378:metabolism*; D008297:Male; D011485:Protein Binding; D051381:Rats; D017207:Rats, Sprague-Dawley
chemical_list: D008070:Lipopolysaccharides; D008077:Lipoproteins, LDL