Purification of Antiestrogen Binding Site by Affinity Chromatography

Abstract

Antiestrogen binding protein has been purified from mouse mammary gland microsomal membranes by affinity chromatography on epoxy activated tamoxifen sepharose. The purification achieved was about 200-fold. The molecular weight of the protein as determined by SDS-PAGE was 90,000 daltons. The protein was also immunoprecipitable by anti-prolactin receptor Antibody

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