[Purification of bovine antimullerian hormone using a monoclonal antibody]

Bovine antimüllerian hormone (AMH) has been purified from incubation medium of bovine fetal testes, by immunoaffinity chromatography using a monoclonal antibody. Presence of AMH in the column eluate is demonstrated by its high antimüllerian activity. Biochemical analysis, by SDS polyacrylamide gel electrophoresis, indicates that the testicular protein eluted from the column co-electrophoreses with native tritiated AMH which, as previously shown, is a dimer of 124,000 +/- 15,000 MW.