Molecular weights of estrogen and androgen binding proteins in the liver of Xenopus laevis.
[3-H]Estradiol-17beta and [3-H]dihydrotestosterone binding proteins in the cytosol fraction of liver from both male and female Xenopus laevis were characterized by electrophoresis on polyacrylamide gels. These binding proteins, which were indistinguishable based upon their mobilities on gels of different acrylamide concentrations, migrated as single components with a molecular weight of 2.0 x 10-4. Separation of native or sodium dodecyl sulfate denatured specific estrogen-binding components on dodecyl sulfate free acrylamide gels gave similar results, i.e., a single species of molecular weight 2.0-2.5 x 10-4. The same molecular weight also was obtained when cytosol was prepared in the presence of either diisopropyl fluorophosphate or phenylmethanesulfonyl fluoride, protease inhibitors. Evidence that the liver components binding either [3-H]estradiol-17-beta or [3-H]dihydrotestosterone were not plasma contaminants was provided by the observation that the plasma sex-steroid binding globulin of Xenopus had a different mobility when separated by polyacrylamide gel electrophoresis.
D000818:Animals; D001665:Binding Sites; D003600:Cytosol / Q000378:metabolism; D013196:Dihydrotestosterone / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004958:Estradiol / Q000378:metabolism*; D005260:Female; D007531:Isoflurophate; D008099:Liver / Q000378:metabolism*; D008297:Male; D008698:Mesylates; D008970:Molecular Weight; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism; D011956:Receptors, Cell Surface; D012967:Sodium Dodecyl Sulfate; D013997:Time Factors; D014981:Xenopus
D008698:Mesylates; D011506:Proteins; D011956:Receptors, Cell Surface; D013196:Dihydrotestosterone; D007531:Isoflurophate; D012967:Sodium Dodecyl Sulfate; D004958:Estradiol