Literature DB >> 838115

Purification of oestradiol receptor from human uterus by affinity chromotrgraphy.

A I Coffer, P J Milton, J Pryse-Davies, R J King.   

Abstract

The oestrogen receptor from human myometrium has been extensively purified by affinity chromatography and isoelectric focusing. The latter step is necessary to remove contaminating sex-steroid-binding globulin. The unpurified 3.7-S cytoplasmic receptor has a molecular weight of 41,000, a Stokes radius of 27.0 A and a frictional ratio (f/f0) of 1.19; the KD (4 degrees C) for [3H]oestradiol-17 beta was 1.03 X 10(-10) M. After purification, the molecular weight was 30,000, the Stokes radius 23.6 A, frictional ratio 1.15 and isoelectric point 6.15.

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Year:  1977        PMID: 838115     DOI: 10.1016/0303-7207(77)90098-3

Source DB:  PubMed          Journal:  Mol Cell Endocrinol        ISSN: 0303-7207            Impact factor:   4.102


  3 in total

1.  Purification and characterization of biologically active scatter factor from ras-transformed NIH 3T3 conditioned medium.

Authors:  A Coffer; J Fellows; S Young; D Pappin; D Rahman
Journal:  Biochem J       Date:  1991-08-15       Impact factor: 3.857

2.  "Affinity" chromatography of steroid-transforming enzymes with a non-steroidal ligand.

Authors:  A G Renwick; S M Chambers; P Willcox
Journal:  Biochem J       Date:  1979-02-01       Impact factor: 3.857

3.  The prognostic value of the monoclonal antibody (D5) detected protein, p29, in primary colorectal carcinoma.

Authors:  J F Robertson; D L Morris; I O Ellis; N C Armitage; J D Hardcastle
Journal:  Br J Cancer       Date:  1991-08       Impact factor: 7.640

  3 in total

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