Interaction of steroid-binding serum proteins with concanavalin A-Sepharose 4B.
The interaction between steroid-finding serum proteins and concanavalin A was studied using affinity chromatography on concanavalin A-Sepharose 4B. The sex hormone-binding globulins of man and rabbit together with the corticosteroid-binding globulins of man, rabbit and guinea pig were all bound quantitatively by the affinity medium. Only two thirds of rat corticosteriod-binding globulin showed an affinity for concanavalin 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 concanavalin A-Sepharose 4B. Affinity chromatography on concanavalin A-Sepharose 4B is documented to be a valuable supplement to existing methods for analysing steroid-protein interactions.
D000818:Animals; D002352:Carrier Proteins / Q000097:blood*; D002846:Chromatography, Affinity; D003208:Concanavalin A; D013196:Dihydrotestosterone / Q000378:metabolism; D005260:Female; D006168:Guinea Pigs; D006801:Humans; D006854:Hydrocortisone / Q000378:metabolism; D011247:Pregnancy; D011374:Progesterone / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D012685:Sepharose; D012738:Sex Hormone-Binding Globulin / Q000378:metabolism; D014156:Transcortin / Q000378:metabolism
D002352:Carrier Proteins; D012738:Sex Hormone-Binding Globulin; D013196:Dihydrotestosterone; D003208:Concanavalin A; D011374:Progesterone; D014156:Transcortin; D012685:Sepharose; D006854:Hydrocortisone