Protein Purification Using a Soluble Affinity Matrix: Purification of Estrogen Receptor with Estradiol- Polylysine Conjugate
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| 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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