| Abstract: | 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. |
