Interaction of steroid-binding serum proteins with concanavalin A-Sepharose 4B.
Interaction of steroid-binding serum proteins with concanavalin A-Sepharose 4B.
复制标题
类固醇结合血清蛋白与刀豆球蛋白 A-Sepharose 4B 的相互作用。
作者：
O. Lea
采用魔豆蛋白A- sepharose 4B亲和层析的方法研究了甾体检测血清蛋白与魔豆蛋白A的相互作用。人、兔的性激素结合球蛋白和人、兔、豚鼠的皮质激素结合球蛋白均被亲和力培养基定量结合。只有三分之二的大鼠皮质类固醇结合球蛋白显示出与豆豆蛋白A的亲和力，表明该蛋白在末端甘露糖或葡萄糖残基方面是异质的。妊娠豚鼠血清中的黄体酮结合球蛋白是所研究蛋白中碳水化合物含量最高的，不与豆豆蛋白A-Sepharose 4B结合。刀豆蛋白a - sepharose 4B的亲和层析被证明是对现有分析类固醇-蛋白质相互作用方法的有价值的补充。
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.