Purification and properties of squirrel monkey (Saimiri sciureus) corticosteroid binding globulins

Corticosteroid binding globulin (CBG), a serum glycoprotein which binds glucocorticoids and progestins with high affinity, is widely distributed throughout the animal world. Although its charge and size characteristics have largely been conserved across species, the authors found the behavior of CBG in squirrel monkey (Saimiri sciureus) serum during fractionation by polyacrylamide gel electrophoresis or Sephadex chromatography was consistent with a molecule about twice the size of that found in most species. To more fully understand the basis for this difference, they purified the protein by sequential affinity and DEAE-Sepharose chromatographies. The final product was obtained in greater than 60% yield and was found to migrate as a single homogeneous band when examined by electrophoresis. The steroid binding specificity of the purified protein was identical with that of the protein in the starting serum. In contrast to the single protein band observed following electrophoresis under normal conditions, separations in the presence of sodium dodecyl sulfate (SDS) resolved the pure protein into two bands: one at 54,000 daltons and one at 57,000 daltons. Unlike other species, squirrel monkey CBG exists as a dimer in its native state. Antibodies were generated against the purified material and tested for cross-reactivity against the sera from other species by both radioimmunodiffusion and radioimmunoassay techniques. Only serum from titi monkeys was observed to cross-react when examined by radioimmunoassay. Taken together, the results suggest that New World monkey CBG's are distinct from those of other species in both size and immunologic characteristics