Abstract:
:Mouse uterine estrogen receptor (ER) was purified about 11,000-fold from normal mouse uteri by affinity chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified ER demonstrated a major component of 65,000 mol wt with minor fragments of the 54,000- and 37,000-dalton species, as judged by affinity labeling with [3H]tamoxifen aziridine and immunodetection with an ER monoclonal antibody (H-222). The minor fragments were not detected with additional monoclonals (H-226 or D-547), which recognize different domains on the ER molecule. Two-dimensional gel electrophoresis revealed that the major component with a mol wt of 65,000 had a pI of about 6.5. The 54,000- and 37,000-dalton components had similar pI values. Saturation binding and Scatchard plot analysis of purified ER yielded one class of binding sites with an apparent dissociation constant of about 1.4 nM. Changes in the hormonal status resulted in changes in the size of the ER even in the presence of molybdate and leupeptin.
journal_name
Endocrinologyjournal_title
Endocrinologyauthors
Horigome T,Golding TS,Quarmby VE,Lubahn DB,McCarty K Sr,Korach KSdoi
10.1210/endo-121-6-2099subject
Has Abstractpub_date
1987-12-01 00:00:00pages
2099-111issue
6eissn
0013-7227issn
1945-7170journal_volume
121pub_type
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