Interaction of Steroid-Binding Serum Proteins with Concanavalin A-Sepharose 4B

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Abstract
The interaction between steroid-binding serum proteins and concanavalin [Con] A was studied using affinity chromatography on Con A-Sepharose 4B. The sex hormone-binding globulins of man and rabbit together with the corticosteroid-binding globulins [CBG] of man, rabbit and guinea pig were all bound quantitatively by the affinity medium. Only 2/3 of rat CBG showed an affinity for Con A indicating this protein to be heterogeneous with respect to terminal mannose or glucose residues. The progesterone-binding globulin in pregnant guinea pig serum, possessing the highest carbohydrate content of the proteins investigated, did not bind to Con A-Sepharose 4B. Affinity chromatography on Con A-Sepharose 4B is documented to be a valuable supplement to existing methods for analyzing steroid-protein interactions.