Work

Chemical and Antigenic Properties of Pure 108,000 Molecular Weight Chick Progesterone Receptor*

Year: 1987

Type: article

Abstract: Previous purifications of the progesterone receptor have yielded inadequate amounts of pure protein along with significant amounts of a nonreceptor contaminant. We have taken advantage of the high yield provided by an affinity chromatography method for partial purification and after the incorporation of additional steps, we obtained purified progesterone receptor devoid of detectable contaminants and suitable for chemical analysis. A polyclonal antibody was obtained using the pure receptor as the antigen. The antibody was specific for progesterone-binding receptor. Tissue distribution of cross-reacting material, analyzed by immunoblotting, confirmed the presence of the receptor protein only in the two tissues where progesterone binding has been described in the chick: the oviduct and the bursa of Fabricius. It was absent in receptor-negative tissues such as liver and lung. The receptor was cleaved with cyanogen bromide and trypsin to obtain fragments that were partially sequenced.

Source: Molecular Endocrinology

DOI: 10.1210/mend-1-3-249

Authors: Mariel Birnbaumer, Maria Victoria Hinrichs-Rosello, Richard G. Cook, William T. Schrader, Bert W. O’Malley

Institutions: Howard Hughes Medical Institute, 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: bronze

Funder: Eunice Kennedy Shriver National Institute of Child Health and Human Development

Award: G4385198559