Anouassi A, Combarnous Y, Lecompte F, Cahoreau C, Guillou F
Institut National de la Recherche Agronomique, Unité Mécanismes d'Action des Hormones et Gamétogenèse, Nouzilly, France.
Biochimie. 1987 Jun-Jul;69(6-7):647-54. doi: 10.1016/0300-9084(87)90184-2.
Luteinizing hormone (LH) has been purified from 150 dromedary pituitaries and its partial physicochemical, biological and immunological characterization has been achieved. Purification of the hormone was monitored by a porcine LH radioreceptor assay (RRA). In this system, the final camLH preparation exhibited an activity 0.6-fold that of highly purified porcine LH. The acid half-dissociation of camLH at equilibrium was observed at pH 4.2. A homologous camLH RRA was developed using the testicular plasma membrane fraction from prepubertal camels and radioiodinated, highly-purified camLH. Pituitary and chorionic gonadotropins (CG) from several mammalian species were compared to camLH in this system. The equine gonadotropins eLH and eCG were shown to be 6 times less potent in the camel RRA than in the porcine RRA, whereas the LH from other species exhibited similar activities in both systems. This particularity of camel LH receptors offers a new tool for the study of structural features of gonatropin interactions with their receptors.
