Work

Progesterone-binding components of chick oviduct. Receptor B subunit protein purified to apparent homogeneity from laying hen oviducts.

Year: 1977

Type: article

Abstract: The progesterone receptor B subunit has been purified to apparent homogeneity from hen oviduct cytosol using ammonium sulfate precipitation and chromatography on DEAE-cellulose, phosphocellulose, hydroxylapatite, and gel filtration on Agarose A-1.5m. The material is obtained (1 mug of purified protein/g of tissue) in about 17% yield. The protein is highly purified; a single band is seen on gel electrophoresis in acid-urea and sodium dodecyl sulfate gels as well as gel electrophoresis under nondenaturing conditions. In the latter system, labeled progesterone co-migrates with the protein band, demonstrating that the isolated protein is a progesterone-binding species. Labeled progesterone bound to the protein is displaced by progestational steroids but not by estradiol or hydrocortisone. The protein has a molecular weight of 116,000 g/mol as determined by gel electrophoresis and has a single polypeptide chain. The isolated protein contains 98% endogenous nonradioactive progesterone and is 2% labeled by incubation in vitro with radiolabeled progesterone. It behaves identically on all of the chromatographic steps to chick receptor B subunits described in earlier publications.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(17)32832-6

Authors: W T Schrader, R W Kuhn, B W O'Malley

Institutions: University of California, San Francisco, Baylor College of Medicine

Language: English

Topic: Estrogen and related hormone effects

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: Muscular Dystrophy Association, National Institutes of Health