Abstract
An alternative to affinity chromatography purification of proteins based on the use of a water-soluble biospecific polymer has been applied to the estrogen receptor from calf uterus. The receptor (4S-trypsin form) was bound to a dextran-estradiol conjugate (molecular weight approximately 500,000) and the complex was isolated by gel filtration. Highly purified receptor was subsequently released from the dextran-estradiol conjugate by exchange with [3H]estradiol.
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