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The binding and uptake of oxidatively modified low density lipoprotein (OxLDL) by mouse peritoneal macrophages occurs, in part, via the well characterized acetyl LDL receptor. However, several lines of evidence indicate that as much as 30-70% of the uptake can occur via a distinct receptor that recognizes OxLDL with a higher affinity than it recognizes(More)
Reduced hepatic membrane receptors for acetylated low-density lipoprotein (acetyl-LDL) and maleylated BSA (Mal-BSA) with apparent molecular masses of 35 kDa, 85 kDa and 15 kDa have been extracted from rat liver and separated by affinity chromatography as described by us previously [Ottnad, Via, Sinn, Freidrich, Ziegler & Dresel (1990) Biochem. J. 265,(More)
The binding characteristics of reduced hepatic membrane proteins for acetylated low-density lipoprotein (acetyl-LDL) and maleylated bovine serum albumin (Mal-BSA) have been examined. Two receptor activities were extracted from hepatic membranes in the presence of octyl beta-D-glucoside and beta-mercaptoethanol, and were separated by chromatography on(More)
Membranes from rat liver were analysed under reducing conditions. The components of the soluble membranes responsible for the binding of acetylated low density lipoprotein (acetyl-LDL) and maleylated bovine serum albumin (Mal-BSA) were chromatographed on a polyethyleneimine-cellulose column and subsequently separated by gel electrophoresis. For both ligands(More)
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