STEROID-PROTEIN INTERACTIONS.
Abstract
Studies on the binding of progesterone to alpha-1-acid glycoprotein were continued. A decreasing effect of traces of heavy metals, especially Fe(++), on the binding affinity was observed. Complete deionization of the test system is necessary. Purification of human corticosteroid-binding blobulin (CBG) by DEAE cellulose chromatography and hydroxylapatite adsorption procedures resulted in an overall concentration of about 700-fold. Application of similar chromatographic techniques, including sephadex G-200 fractionation, to rabbit serum yielded preparations that were purified approximately 2000-fold. Sera of man, monkey, rat, rabbit and guinea pig were freed of endogenous corticosteroids by sephadex filtration at 45C. The binding affinities of these sera were then determined by multiple equilibrium dialysis at five concentrations each of cortisol, corticosterone and progesterone, at 4C and 37C. Concentrations of corticosteroid-binding sites and their association constants were determined. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- May 31, 1965
- Accession Number
- AD0618513
Entities
People
- Ulrich F. Westphal
Organizations
- University of Louisville