Use of fast protein liquid chromatography in the purification of inhibin from bovine follicular fluid
Autor: | Simon van Dijk, Frank H. de Jong, Henk J. van der Molen |
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Rok vydání: | 1984 |
Předmět: |
endocrine system
Chromatography Size-exclusion chromatography Biophysics Fast protein liquid chromatography Exudates and Transudates Cell Biology Biochemistry Follicular fluid chemistry.chemical_compound Ovarian Follicle chemistry Affinity chromatography Sephadex Electroelution Animals Cattle Female Inhibins Sodium dodecyl sulfate Molecular Biology Polyacrylamide gel electrophoresis Chromatography Liquid |
Zdroj: | Biochemical and Biophysical Research Communications. 125:307-314 |
ISSN: | 0006-291X |
DOI: | 10.1016/s0006-291x(84)80369-1 |
Popis: | Inhibin from bovine follicular fluid was partly purified using affinity chromatography on immobilized Procion Red 3B, gel filtration on Sephadex G-25 and ion-exchange chromatography on the fast protein liquid chromatography system. Inhibin was subsequently characterized using preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution. Biological activity was associated with a protein with an apparent molecular weight of approximately 65 kD. |
Databáze: | OpenAIRE |
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