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Comparative structural analyses of corticosteroid binding globulin.

E A Kato1, B R Hsu, R W Kuhn

  • 1Department of Obstetrics, Gynecology and Reproductive Sciences, University of California, San Francisco 94143.

Journal of Steroid Biochemistry
|February 1, 1988
PubMed
Summary
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Corticosteroid binding globulin (CBG) molecular weights vary across species, with squirrel monkeys showing a significantly larger size. Despite conserved peptide patterns, surface differences exist between human, rat, and guinea pig CBG proteins.

Area of Science:

  • Biochemistry
  • Comparative Biology
  • Protein Science

Background:

  • Corticosteroid binding globulin (CBG) plays a crucial role in regulating corticosteroid bioavailability.
  • Understanding species-specific variations in CBG structure is essential for comparative endocrinology.

Purpose of the Study:

  • To determine the physicochemical properties of corticosteroid binding globulin (CBG) across various species.
  • To investigate the structural similarities and differences of purified CBG from human, rat, and guinea pig.

Main Methods:

  • Molecular weight determination using Ferguson plots and sucrose density gradient centrifugation.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for purified CBG.
  • Reversed-phase high-performance liquid chromatography (RP-HPLC) for tryptic peptide analysis.

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  • Amino-terminal sequence analysis and immunological cross-reactivity assays.

    • Main Results:

    • CBG molecular weights ranged from 44,200 (dog) to 60,000 (turtle), with squirrel monkey CBG being exceptionally large (119,800).
    • Purified human, rat, and guinea pig CBG showed consistent molecular weights with Ferguson analysis and comprised two electrophoretic variants.
    • Tryptic peptide patterns were largely identical across species, with minor variations in three hydrophilic peptides.
    • No significant amino-terminal sequence homology or immunological cross-reactivity was found between human, rat, and guinea pig CBG.

    Conclusions:

    • CBG molecular size and peptide hydrophobicity are conserved across species.
    • Significant surface differences exist in CBG proteins despite conserved molecular characteristics.
    • These findings highlight evolutionary divergence in CBG structure and function.