title: Purification, monoclonal antibody production and structural analyses of human progesterone receptors.
abstract: Progesterone receptors (PR) from human breast cancer cells have been purified, and used as antigens to generate anti-PR monoclonal antibodies. Immunologic and in situ photoaffinity labeling methods were then used to study receptor structure, and we conclude that native human PR consist of two independent 8S receptors: one 8S subtype contains B-proteins (120,000 kDa) and the other contains A-proteins (94,000 kDa).
authors.affiliation: University of Colorado Health Sciences Center, Denver, CO 80220.
authors.forename: K B
authors.initials: KB
authors.lastname: Horwitz
mesh_terms: D000345:Affinity Labels; D000911:Antibodies, Monoclonal / Q000276:immunology*; D015153:Blotting, Western; D002846:Chromatography, Affinity; D006801:Humans; D008970:Molecular Weight; D011980:Receptors, Progesterone / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D014407:Tumor Cells, Cultured
chemical_list: D000345:Affinity Labels; D000911:Antibodies, Monoclonal; D011980:Receptors, Progesterone