Biosynthesis of labelled anti-müllerian hormone by fetal testes: evidence for the glycoprotein nature of the hormone and for its disulfide-bonded structure.

Tritiated fucose incorporated into proteins released by fetal calf tests into incubation medium proved to be a marker for anti-müllerian hormone (AMH) once non-specific glycoproteins had been eliminated by partial purification. When partially purified incubation medium from fetal calf teste s was fractionated by gel filtration, sucrose density gradient sedimentation or preparative electrofocusing, a single radioactive protein peak co-purified with anti-müllerian activity. Partially purified medium from bull testes--which are devoid of anti-müllerian activity--has a much lower fucose content than that derived from fetal testes. Antisera directed against 'fetal'--but not 'bull'--partially purified incubation medium, and capable of blocking anti-müllerian activity, precipitated the radioactive protein peak. The molecular weight of labelled AMH was 215,000 when determined by gel filtration and 124,000 when determined by density gradient sedimentation. By SDS-PAGE the molecular weight of labelled AMH was 123,000 and dissociation into a 72,000 subunit was demonstrated under conditions which reduce disulfide bonds.