PMID: 6538858Jan 1, 1984Paper

Binding of progesterone with the oviduct cytosol fraction of estrogen-primed quail (Coturnix coturnix japonica)

General and Comparative Endocrinology
M Agemori, K Ishikawa

Abstract

Progesterone-specific binding components were detected in the cytosol fraction of enlarged oviducts from estrogen (diethylstilbestrol)-primed immature Japanese quail (Coturnix coturnix japonica) females by several techniques using [3H]promegestone. The oviduct as a target tissue of progesterone is the most efficient in [3H]promegestone binding, and muscle and intestine as nontarget tissues and plasma are less efficient as expected. By using [3H]promegestone for binding, the possibility of blood contamination of the oviduct may have been eliminated with the detection of a specific binding site. The participation of protein in the steroid-binding site was inferred from the destruction of the binding component by protease, but not by RNase or DNase. The interaction with [3H]promegestone in low salt conditions has a high affinity (Kd 0.69 nM) and low capacity (the number of binding sites per milligram of protein is about 1.3 pmol). Six unlabeled steroids were tested as competitors for binding to [3H]promegestone in vitro. Progesterone-like steroids competed specifically with [3H]promegestone: progesterone congruent to promegestone greater than deoxycorticosterone greater than testosterone much greater than estradiol-17 beta greater...Continue Reading

References

Feb 1, 1975·Biology of Reproduction·W T SchraderB W O'Malley
Mar 11, 1977·Annals of the New York Academy of Sciences·M R Sherman, S C Diaz
Feb 1, 1978·General and Comparative Endocrinology·R T Turner, L P Eliel
Feb 15, 1974·Science·B W O'Malley, A R Means
Mar 1, 1974·Endocrinology·D Philibert, J P Raynaud
Jun 1, 1981·General and Comparative Endocrinology·J K KorpelaP J Tuohimaa
Nov 1, 1980·Journal of Biochemistry·A MurayamaT Yamamoto

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Citations

Jan 3, 2009·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·Arie Bar

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