STEROID-PROTEIN INTERACTIONS. XI. ELECTROPHORETIC CHARACTERIZATION OF CORTICOSTEROID-BINDING PROTEINS IN SERUM OF RAT, MAN AND OTHER SPECIES,
Abstract
A study was undertaken to determine whether one or more serum protein component is responsible for the high-affinity binding of different corticosteroids and to characterize the corticosteroid-binding proteins of several mammalian sera. The highest binding affinity for cortiocosterone, cortisol or aldosterone was observed with the same electrophoretic fraction of human serum. Cortisol displaced aldosterone from its binding sites. In rat serum an electrophoretic component was responsible for high-affinity binding of corticosterone and cortisol. In the serum of rat and rabbit the alpha-1-globulin fraction showed the highest specific activity for corticosterone-4-C14 and cortisol-4-C14. For bovine and horse serum the highest binding affinity was associated with the alpha-globulin fraction. The high-affinity corticosteroid-binding proteins in several mammalian sera are thus alpha-globulins. Low pH values affect the migration of the corticosteroid-binding globulin of rat serum in the electrophoretic field as a prealbumin. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 13, 1965
- Accession Number
- AD0627304
Entities
People
- Frank De Venuto
- Ulrich F. Westphal
Organizations
- University of Louisville