Accession Number:

AD0627304

Title:

STEROID-PROTEIN INTERACTIONS. XI. ELECTROPHORETIC CHARACTERIZATION OF CORTICOSTEROID-BINDING PROTEINS IN SERUM OF RAT, MAN AND OTHER SPECIES,

Descriptive Note:

Corporate Author:

LOUISVILLE UNIV KY SCHOOL OF MEDICINE

Personal Author(s):

Report Date:

1965-09-13

Pagination or Media Count:

25.0

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

Subject Categories:

  • Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE