Protein Purification Using a Soluble Affinity Matrix: Purification of Estrogen Receptor with Estradiol- Polylysine Conjugate
EPrints@IICB
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Title |
Protein Purification Using a Soluble Affinity Matrix: Purification of Estrogen Receptor with Estradiol- Polylysine Conjugate
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Creator |
Bhattacharjee, Maitreyi
Ali, Esahak |
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Subject |
Infectious Diseases and Immunology
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Description |
A new strategy for protein purification using a soluble affinity matrix is described. The method was used for purification of estrogen receptor. Cytosols from rat uteri and human fibroid uterine tissue, after fractionation by ammonium sulfate, were treated with estradiol- polylysine conjugate. The highly basic affinity complex was separated from other proteins by DEAESephacel chromatography. After dissociation of the eluted complex with excess estradiol, the receptor was recovered by CM-Sephadex chromatography. A 2000- fold purification of the rat uterine estrogen receptor was obtained with an activity recovery of 35%. |
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Publisher |
Elsevier
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Date |
1992
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Identifier |
http://www.eprints.iicb.res.in/1784/1/ANALYTICAL_BIOCHEMISTRY___201(_2)_233%2D236;1992[51].pdf
Bhattacharjee, Maitreyi and Ali, Esahak (1992) Protein Purification Using a Soluble Affinity Matrix: Purification of Estrogen Receptor with Estradiol- Polylysine Conjugate. Analytical Biochemistry, 201 (2). pp. 233-236. |
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Relation |
http://dx.doi.org/10.1016/0003-2697(92)90333-3
http://www.eprints.iicb.res.in/1784/ |
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