PURIFICATION OF BOVINE ANTI-MULLERIAN HORMONE USING A MONOCLONAL-ANTIBODY

1 January 1981

journal article
research article

Vol. 293 (8) , 447-450

Abstract

Bovine antimuellerian hormone (AMH) was 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 antimuellerian activity. Biochemical analysis, by sodium dodecyl sulfate polyacrylamide gel electrophoresis, indicates that the testicular protein eluted from the column co-electrophoresis with native tritiated AMH which, as previously shown, is a dimer of 124,000 .+-. 15,000 MW.

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