Serum of the pregnant donkey, like that of the mare, contains a gonadotrophin of chorionic origin. The chorionic gonadotrophin of the donkey (dCG) has been isolated in purified form from the serum of pregnant donkeys using methodology previously employed for the purification of pregnant mare chorionic gonadotrophin (eCG). Unlike eCG, dCG is predominantly an LH in biological tests. In the in-vitro rat Leydig cell assay, dCG was as active as eCG, but in the in-vitro rat seminiferous tubule assay for FSH and in the augmentation assay, dCG was considerably less potent than eCG (1–10%). Specific rat testis radioreceptor assays for LH and FSH also showed dCG to be at least nine times more potent in LH than in FSH activity. Chemically, dCG was found to be similar to eCG in fractionation behaviour and glycoprotein nature. However, dCG had significantly less carbohydrate (31%) than had eCG (45%) and several differences were noted in a comparison of amino-acid compositions. A single amino-terminal residue, phenylalanine, was detected in dCG. Immunologically, dCG cross-reacted in homologous radioimmunoassays for eCG, equine LH and equine FSH, but its inhibition curves were all non-parallel with those of the respective equine gonadotrophin standards.
Purification and Characterization of the Amino-Terminal Domain of Lumazine Protein from Photobacterium leiognathi