6533b829fe1ef96bd128adc8

RESEARCH PRODUCT

Preparation of electrophoretic variants of Corticosteroid-binding Globulin (CBG) using liquid liquid partition chromatography

A. HeubnerKunhard PollowM. Juchem

subject

TranscortinPharmacologyAmmonium sulfateChromatographybiologyGlobulinChemistryElutionOrganic ChemistryClinical BiochemistryFractionationBiochemistryChromatography AffinitySepharoseElectrophoresischemistry.chemical_compoundEndocrinologyTranscortinAffinity chromatographybiology.proteinHumansElectrophoresis Polyacrylamide GelMolecular BiologyChromatography Liquid

description

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.

yearjournalcountryeditionlanguage
1988-10-01Steroids
https://doi.org/10.1016/0039-128x(88)90175-4