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
Rok vydání: 1984
Předmět:
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