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- W2062547513 abstract "Human corticosteroid-binding globulin (CBG) was purified to homogeneity by application of three different chromatographic methods. After fractionation of pregnancy serum with ammonium sulfate the 80%-pellet was used for affinity chromatography based on tresyl activated Sepharose (Pharmacia, Uppsala, Sweden). The affinity eluate was injected into a Mono Q anion exchange column (Pharmacia). Fractions containing CBG were finally purified by liquid liquid chromatography on LiParGel 750 (Merck, Darmstadt, F.R.G.) 1,2 . The purified protein was characterized by IEF and PAGE. This paper describes a method for the chromatographic separation of the two variants of CBG without a loss of binding activity towards steroids for each of the two characteristic bands of this protein." @default.
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- W2062547513 date "1988-10-01" @default.
- W2062547513 modified "2023-09-30" @default.
- W2062547513 title "Preparation of electrophoretic variants of Corticosteroid-binding Globulin (CBG) using liquid liquid partition chromatography" @default.
- W2062547513 cites W1480579302 @default.
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- W2062547513 doi "https://doi.org/10.1016/0039-128x(88)90175-4" @default.
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