PMID: 7087792Jul 1, 1982Paper

Oviduct progesterone receptor: physical and chemical studies

Metabolism: Clinical and Experimental
W T Schrader

Abstract

Chicken oviduct progesterone receptor has been purified to homogeneity. The protein consists of two dissimilar hormone-binding subunits, A and B, present in equal amounts in the complex. They have molecular weights of 79,000 and 108,000, respectively, as shown by both SDS-gel electrophoresis of the purified proteins and photoaffinity labeling of both with a labeled synthetic progestin. The two subunits show considerable homology (or identity) of structure at the hormone-binding domain, located at the N-terminus of the proteins. Considerable divergence of sequence must exist elsewhere in A and B, as shown by tryptic peptide mapping and by the fact that subunit A has a strong DNA-binding site lacking in B. Both are phosphorylated in vitro by cAMP-dependent protein kinase; this phosphorylation appears to be responsible for creation of a second, weaker progesterone-binding site on each subunit.

References

Jan 1, 1979·Journal of Steroid Biochemistry·W A CotyB W O'Malley
Oct 1, 1976·Journal of Steroid Biochemistry·P E HansenB W O'Malley
Sep 16, 1981·Biochemical and Biophysical Research Communications·N L WeigelB W O'Malley
Dec 1, 1981·Journal of Steroid Biochemistry·A MaggiB W O'Malley

Citations

Jan 1, 1984·Journal of Steroid Biochemistry·J G ComptonB W O'Malley

Related Concepts

SDS-PAGE
Animal Oviduct
Phosphoproteins
Receptors, Progesterone

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