Soluble biospecific macromolecule for purification of estrogen receptor.

Abstract
An alternative to affinity chromotography purification of proteins based on the use of a water-soluble biospecific polymer was applied to the estrogen receptor from calf uterus. The receptor (4S-trypsin form) was bound to a dextran-estradiol conjugate (MW .apprx. 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.