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pubmed-article:1917521pubmed:abstractTextLipoproteins were isolated either by immunoaffinity chromatography (LDL and VLDL) or ultracentrifugation (LDL). Purified lipoproteins were labeled with 123I using either Iodogen or iodine-monochloride (IC1) each followed by purification with gel-chromatography or dialysis (total of 4 combinations). Lipoprotein-concentrations of 0.1-6 micrograms protein/mL were used for direct binding assays investigating the specific binding of labeled lipoproteins (in the presence of a 50-fold excess of unlabeled lipoproteins) to human liver apo-B, E-receptors. In separate experiments displacement of bound 123I-lipoproteins (labeled by the methods mentioned) by unlabeled ones was studied. The binding capacities estimated by Scatchard analysis were similar to each other (141-163 ng protein bound/mg liver plasma membrane protein) independent from the method used for isolation and labeling. Also the affinity constants were very similar and ranged from 0.9 to 1.7 micrograms protein/L. It is concluded that immunoaffinity chromatography or ultracentrifugation for isolation of lipoproteins and the Iodogen or IC1-method for radiolabeling can be recommended to be equally good for in vitro receptor investigation.lld:pubmed
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pubmed-article:1917521pubmed:pagination513-7lld:pubmed
pubmed-article:1917521pubmed:dateRevised2008-2-21lld:pubmed
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pubmed-article:1917521pubmed:year1991lld:pubmed
pubmed-article:1917521pubmed:articleTitleComparison of different methods for LDL isolation and radioiodination on liver LDL receptor binding in vitro.lld:pubmed
pubmed-article:1917521pubmed:affiliationAtherosclerosis Research Group (ATK), Austrian Academy of Sciences.lld:pubmed
pubmed-article:1917521pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1917521pubmed:publicationTypeComparative Studylld:pubmed
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