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.
D000818:Animals; D002417:Cattle; D004220:Disulfides; D005260:Female; D005333:Fetus; D005643:Fucose / Q000378:metabolism; D007106:Immune Sera; D007118:Immunoassay; D008297:Male; D008970:Molecular Weight; D009095:Mullerian Ducts / Q000254:growth & development / Q000378:metabolism; D011247:Pregnancy; D013735:Testicular Hormones / Q000096:biosynthesis*; D013737:Testis / Q000378:metabolism*; D013961:Thyroid Gland / Q000378:metabolism*
D004220:Disulfides; D007106:Immune Sera; D013735:Testicular Hormones; D005643:Fucose