[Isolation of a pituitary receptor for gonadoliberin (GnRH) in a highly purified state].
Using a gonadoliberin (GnRH) receptor preparation from the bovine pituitaries, we purified the receptor approximately 14,000 fold as compared to the starting material, with a overall yield of about 40%. The binding capacity of a iodinated GnRH analog, used for radioreceptor assay, increased from 16 fmoles/mg of protein in the crude material to 225 pmoles/mg of protein in the final product. The affinity constant was not modified by the purification process and remained close to Ka = 10(10) M-1. Electrophoretic analysis of the purified preparation suggests an apparent molecular mass of about 60,000 Da for the receptor.
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010903:Pituitary Gland, Anterior / Q000032:analysis*; D011869:Radioligand Assay; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D011966:Receptors, LHRH
D011956:Receptors, Cell Surface; D011966:Receptors, LHRH
Obtention du récepteur hypophysaire de la gonadolibérine (GnRH) à l'état hautement purifié.