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Purification and properties of squirrel monkey (Saimiri sciureus) corticosteroid binding globulin
R W Kuhn1, C VestWeber, P K Siiteri
1Department of Obstetrics/Gynecology, University of California, San Francisco 94143.
Biochemistry
|April 5, 1988
Summary
Squirrel monkey corticosteroid binding globulin (CBG) exhibits unique size characteristics compared to other species. Purification revealed distinct subunit sizes, suggesting structural variations in this important serum glycoprotein.
Area of Science:
- Biochemistry
- Proteomics
- Comparative biology
Background:
- Corticosteroid binding globulin (CBG) is a serum glycoprotein binding glucocorticoids and progestins.
- CBG's structure is generally conserved across species, but variations exist.
Purpose of the Study:
- To investigate the unique size characteristics of squirrel monkey (Saimiri sciureus) CBG.
- To purify and characterize squirrel monkey CBG to understand structural differences.
Main Methods:
- Sequential affinity and DEAE-Sepharose chromatography for protein purification.
- Polyacrylamide gel electrophoresis (PAGE) under various conditions.
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for subunit analysis.
- Amino acid composition analysis.
Main Results:
- Purified squirrel monkey CBG showed high yield and homogeneity via electrophoresis.
- Steroid binding specificity was consistent with known CBG.
- SDS-PAGE revealed two distinct subunit bands at 54,000 and 57,000 daltons.
- Amino acid composition was similar to other species' CBG but distinct from other proteins.
Conclusions:
- Squirrel monkey CBG possesses unique structural properties, indicated by its distinct subunit molecular weights.
- These findings contribute to understanding the structural diversity of CBG across species.