Soluble biospecific macromolecule for purification of estrogen receptor.
Identifieur interne : 000091 ( Pmc/Curation ); précédent : 000090; suivant : 000092Soluble biospecific macromolecule for purification of estrogen receptor.
Auteurs : P. Hubert ; J. Mester ; E. Dellacherie ; J. Neel ; E E BaulieuSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1978.
Abstract
An alternative to affinity chromatography purification of proteins based on the use of a water-soluble biospecific polymer has been applied to the estrogen receptor from calf uterus. The receptor (4S-trypsin form) was bound to a dextran-estradiol conjugate (molecular weight approximately 500,000) and the complex was isolated by gel filtration. Highly purified receptor was subsequently released from the dextran-estradiol conjugate by exchange with [3H]estradiol.
Url:
PubMed: 277916
PubMed Central: 392730
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<author><name sortKey="Hubert, P" sort="Hubert, P" uniqKey="Hubert P" first="P" last="Hubert">P. Hubert</name>
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<author><name sortKey="Mester, J" sort="Mester, J" uniqKey="Mester J" first="J" last="Mester">J. Mester</name>
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<author><name sortKey="Dellacherie, E" sort="Dellacherie, E" uniqKey="Dellacherie E" first="E" last="Dellacherie">E. Dellacherie</name>
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<author><name sortKey="Neel, J" sort="Neel, J" uniqKey="Neel J" first="J" last="Neel">J. Neel</name>
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<author><name sortKey="Baulieu, E E" sort="Baulieu, E E" uniqKey="Baulieu E" first="E E" last="Baulieu">E E Baulieu</name>
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<author><name sortKey="Neel, J" sort="Neel, J" uniqKey="Neel J" first="J" last="Neel">J. Neel</name>
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<author><name sortKey="Baulieu, E E" sort="Baulieu, E E" uniqKey="Baulieu E" first="E E" last="Baulieu">E E Baulieu</name>
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<series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
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<front><div type="abstract" xml:lang="en"><p>An alternative to affinity chromatography purification of proteins based on the use of a water-soluble biospecific polymer has been applied to the estrogen receptor from calf uterus. The receptor (4S-trypsin form) was bound to a dextran-estradiol conjugate (molecular weight approximately 500,000) and the complex was isolated by gel filtration. Highly purified receptor was subsequently released from the dextran-estradiol conjugate by exchange with [3H]estradiol.</p>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id>
<journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title>
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<title-group><article-title>Soluble biospecific macromolecule for purification of estrogen receptor.</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Hubert</surname>
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<contrib contrib-type="author"><name><surname>Dellacherie</surname>
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<pub-date pub-type="ppub"><month>7</month>
<year>1978</year>
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<volume>75</volume>
<issue>7</issue>
<fpage>3143</fpage>
<lpage>3147</lpage>
<abstract><p>An alternative to affinity chromatography purification of proteins based on the use of a water-soluble biospecific polymer has been applied to the estrogen receptor from calf uterus. The receptor (4S-trypsin form) was bound to a dextran-estradiol conjugate (molecular weight approximately 500,000) and the complex was isolated by gel filtration. Highly purified receptor was subsequently released from the dextran-estradiol conjugate by exchange with [3H]estradiol.</p>
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