Further characterization of the estrogen binding macromolecule in human pancreas
Autor: | Roland Fernstad, Holger Sköldefors, Nils-Olof Theve, Åke Pousette, Kjell Carlström |
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Rok vydání: | 1985 |
Předmět: |
Chromatography
Estradiol Macromolecular Substances Binding protein Estrogen receptor Fast protein liquid chromatography Glutamic acid Biology Chromatography Ion Exchange Biochemistry Molecular Weight Cytosol Endocrinology Receptors Estrogen Humans Electrophoresis Polyacrylamide Gel Estrogen binding Leucine Amino Acids Carrier Proteins Pancreas Histidine |
Zdroj: | Journal of steroid biochemistry. 23(1) |
ISSN: | 0022-4731 |
Popis: | The estrogen binding protein in human pancreas has been purified from pancreatic cytosol by chromatography on Concanavalin-A-Sepharose and hydroxyl-apatite followed by ion-exchange chromatography carried out using a fast-protein liquid chromatography apparatus (FPLC). The purified protein, still able to bind labelled [3H]estradiol, appeared as one single band corresponding to 31 K in SDS-gel electrophoresis. Total amino acid analysis revealed high levels of histidine, glutamic acid and leucine. The capacity of the purified protein to bind estrogens could be increased more than 4-fold by addition of a cytosolic factor, probably being a small peptide, that is present in crude cytosol, but lost during the purification procedure. The iodinated protein does not bind to DNA-cellulose or phosphocellulose, and shows no similarities to estrogen receptor proteins. |
Databáze: | OpenAIRE |
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