| Autor: |
Jansem de Almeida Catanho MT, Bérault A, Théoleyre M, Kochman K, Jutisz M |
| Jazyk: |
francouzština |
| Zdroj: |
Comptes rendus de l'Academie des sciences. Serie III, Sciences de la vie [C R Acad Sci III] 1984; Vol. 298 (7), pp. 177-80. |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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