PURIFICATION OF "INHIBIN" FROM HUMAN OVARIAN FOLLICULAR FLUID

Publisher Website
Google Scholar
Abstract
Following the earlier demonstration of inhibin-like activity in human ovarian follicular fluid a method for its purification to apparent homogeneity was described. The fluid was converted to acetone powder and subjected sequentially to ammonium sulfate fractionation, gel chromatography on Sephadex G-200, continuous gradient ion exchange chromatography on DEAE-cellulose, first with a pH gradient from 8.0-4.0 and then with a NaCl gradient to 1 M at pH 5.2. The active fraction from this step was subjected to gel filtration on Sephadex G-100 and finally passed through an Amicon Centriflo membrane CF-25 (cut off point: 25,000 MW). The ultrafiltrate was homogeneous by SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis, had a MW of the order of 23,000 and was capable of suppressing serum gonadotropin levels in the castrated male rats in as low a dose as 25 .mu.g/rat.

This publication has 1 reference indexed in Scilit: