Isolation and renaturation of alpha 2-macroglobulin receptor from diploid human fibroblasts.
alpha 2-Macroglobulin receptor was extracted from human diploid fibroblasts and purified by affinity chromatography in a single step. The receptor had mol.wt. 125 000 after sodium dodecyl sulphate (SDS)/polyacrylamide-gel electrophoresis. The isolated receptor was separated by SDS/polyacrylamide-gel electrophoresis, transferred on to nitrocellulose sheets and subsequently renatured, as shown by a specific binding test, by incubation with Nonidet P40.
D002846:Chromatography, Affinity; D004171:Diploidy; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000032:analysis*; D006801:Humans; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D011971:Receptors, Immunologic / Q000302:isolation & purification*; D000511:alpha-Macroglobulins
D026503:Low Density Lipoprotein Receptor-Related Protein-1; D011971:Receptors, Immunologic; D000511:alpha-Macroglobulins