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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1990-3-27
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pubmed:abstractText |
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 Mal-BSA-Sepharose 4B. The receptors were revealed by ligand blotting. The active binding proteins had apparent molecular masses of 35 and 15 kDa in SDS/polyacrylamide gels. Equilibrium studies with protein-phosphatidylcholine complexes indicated that the reduced 35 kDa protein expresses two binding sites for Mal-BSA and one for acetyl-LDL, whereas the 15 kDa protein-phosphatidylcholine complex binds 131I-Mal-BSA and 131I-acetyl-LDL with a 4:1 stoichiometry. 131I-Mal-BSA binding was linear with both proteins, with a Kd of 4.8 nM at the 35 kDa protein and a Kd of 5.6 nM at the 15 kDa protein. The 35 kDa protein displayed saturable binding of 131I-acetyl-LDL with a Kd of 5 nM; the 15 kDa binding protein bound 131I-acetyl-LDL with a Kd of 2.3 nM. A 85 kDa protein was obtained by Mal-BSA-Sepharose chromatography when the hepatic membranes had been solubilized with Triton X-100 in presence of GSH/GSSG. This protein displayed saturable 131I-Mal-BSA binding with a Kd of 30 nM and 131I-acetyl-LDL binding with a Kd of 6.5 nM. The 131I-Mal-BSA binding capacity was four times higher than that of 131I-acetyl-LDL. Competition studies with the 35 kDa, 15 kDa and 85 kDa proteins binding Mal-BSA, acetyl-LDL, formylated albumin and polyanionic competitors provide evidence for the existence of more than one class of binding sites at the reduced binding proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-13252080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-184464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-218198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-2845939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-2981213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-3194423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-3389510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-3433016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-3582361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-3965468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-3997875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-4006910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-6086616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-6254970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-6311077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-6313644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-6592955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2154967-7040394
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Albumin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
689-98
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2154967-Acetylation,
pubmed-meshheading:2154967-Animals,
pubmed-meshheading:2154967-Chromatography, Affinity,
pubmed-meshheading:2154967-Chromatography, Gel,
pubmed-meshheading:2154967-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2154967-Humans,
pubmed-meshheading:2154967-Ligands,
pubmed-meshheading:2154967-Lipoproteins, LDL,
pubmed-meshheading:2154967-Liver,
pubmed-meshheading:2154967-Membrane Proteins,
pubmed-meshheading:2154967-Rats,
pubmed-meshheading:2154967-Receptors, Albumin,
pubmed-meshheading:2154967-Receptors, Cell Surface,
pubmed-meshheading:2154967-Receptors, LDL,
pubmed-meshheading:2154967-Serum Albumin, Bovine
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pubmed:year |
1990
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pubmed:articleTitle |
Binding characteristics of reduced hepatic receptors for acetylated low-density lipoprotein and maleylated bovine serum albumin.
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pubmed:affiliation |
Department of Medicine, University of Heidelberg, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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