Purification of dihydrofolic reductase from chicken liver by affinity chromatography
The procedure for coupling methotrexate (4-amino-10-methylpteroylglutamic acid) to Sepharose via a six carbon chain is described. An affinity column prepared from this material quantitatively adsorbs the dihydrofolic reductase activity from a partially purified extract of chicken liver. Elution of t...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1971-08, Vol.44 (3), p.608-613 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 613 |
|---|---|
| container_issue | 3 |
| container_start_page | 608 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 44 |
| creator | Kaufman, Bernard T. Pierce, Jack V. |
| description | The procedure for coupling methotrexate (4-amino-10-methylpteroylglutamic acid) to Sepharose via a six carbon chain is described. An affinity column prepared from this material quantitatively adsorbs the dihydrofolic reductase activity from a partially purified extract of chicken liver. Elution of the enzyme readily occurs with dilute K
2HPO
4 in the presence of dihydrofolate. Approximately 250-fold purification occurs by affinity chromatography yielding a preparation which appears to be homogeneous. |
| doi_str_mv | 10.1016/S0006-291X(71)80126-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_81175934</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X71801262</els_id><sourcerecordid>81175934</sourcerecordid><originalsourceid>FETCH-LOGICAL-c360t-b1a79ba3338bf1d9a99a2023b7ba9614ede727d7148da5997c97615a5602a9473</originalsourceid><addsrcrecordid>eNqFkElLBDEQhYMo47j8BKFPoofWVHrJ5CQyuMGAgiN4C-mk4kR7OmPSLfS_t2fBq6eieO_Voz5CzoBeAYXy-pVSWqZMwPsFh8sJBTZse2QMVNCUAc33yfjPckiOYvykFCAvxYiMCmAZCDEm85cuOOu0ap1vEm8T4xa9Cd762ukkoOl0qyImNvhlohdOf2GT1O4HQ1L1ibLWNa7tB2XQVes_glot-hNyYFUd8XQ3j8nb_d18-pjOnh-eprezVGclbdMKFBeVyrJsUlkwQgmhGGVZxSslSsjRIGfccMgnRhVCcC14CYUqSsqUyHl2TM63d1fBf3cYW7l0UWNdqwZ9F-UEgBciywdjsTXq4GMMaOUquKUKvQQq1zTlhqZco5Ic5IamZEPubFfQVUs0f6kdvkG_2eo4fPnjMMioHTYajQuoW2m8-6fhF1xbhUk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>81175934</pqid></control><display><type>article</type><title>Purification of dihydrofolic reductase from chicken liver by affinity chromatography</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Kaufman, Bernard T. ; Pierce, Jack V.</creator><creatorcontrib>Kaufman, Bernard T. ; Pierce, Jack V.</creatorcontrib><description>The procedure for coupling methotrexate (4-amino-10-methylpteroylglutamic acid) to Sepharose via a six carbon chain is described. An affinity column prepared from this material quantitatively adsorbs the dihydrofolic reductase activity from a partially purified extract of chicken liver. Elution of the enzyme readily occurs with dilute K
2HPO
4 in the presence of dihydrofolate. Approximately 250-fold purification occurs by affinity chromatography yielding a preparation which appears to be homogeneous.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(71)80126-2</identifier><identifier>PMID: 5123199</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Ammonium Sulfate ; Animals ; Chemical Phenomena ; Chemical Precipitation ; Chemistry ; Chickens ; Chromatography ; Chromatography, Gel ; Cyanides ; Folic Acid ; Hydroxyapatites ; Imides ; Liver - enzymology ; Methods ; Methotrexate ; Methylamines ; Polyamines ; Polysaccharides ; Protein Binding ; Tetrahydrofolate Dehydrogenase - isolation & purification</subject><ispartof>Biochemical and biophysical research communications, 1971-08, Vol.44 (3), p.608-613</ispartof><rights>1971</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-b1a79ba3338bf1d9a99a2023b7ba9614ede727d7148da5997c97615a5602a9473</citedby><cites>FETCH-LOGICAL-c360t-b1a79ba3338bf1d9a99a2023b7ba9614ede727d7148da5997c97615a5602a9473</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X71801262$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5123199$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kaufman, Bernard T.</creatorcontrib><creatorcontrib>Pierce, Jack V.</creatorcontrib><title>Purification of dihydrofolic reductase from chicken liver by affinity chromatography</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The procedure for coupling methotrexate (4-amino-10-methylpteroylglutamic acid) to Sepharose via a six carbon chain is described. An affinity column prepared from this material quantitatively adsorbs the dihydrofolic reductase activity from a partially purified extract of chicken liver. Elution of the enzyme readily occurs with dilute K
2HPO
4 in the presence of dihydrofolate. Approximately 250-fold purification occurs by affinity chromatography yielding a preparation which appears to be homogeneous.</description><subject>Ammonium Sulfate</subject><subject>Animals</subject><subject>Chemical Phenomena</subject><subject>Chemical Precipitation</subject><subject>Chemistry</subject><subject>Chickens</subject><subject>Chromatography</subject><subject>Chromatography, Gel</subject><subject>Cyanides</subject><subject>Folic Acid</subject><subject>Hydroxyapatites</subject><subject>Imides</subject><subject>Liver - enzymology</subject><subject>Methods</subject><subject>Methotrexate</subject><subject>Methylamines</subject><subject>Polyamines</subject><subject>Polysaccharides</subject><subject>Protein Binding</subject><subject>Tetrahydrofolate Dehydrogenase - isolation & purification</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1971</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkElLBDEQhYMo47j8BKFPoofWVHrJ5CQyuMGAgiN4C-mk4kR7OmPSLfS_t2fBq6eieO_Voz5CzoBeAYXy-pVSWqZMwPsFh8sJBTZse2QMVNCUAc33yfjPckiOYvykFCAvxYiMCmAZCDEm85cuOOu0ap1vEm8T4xa9Cd762ukkoOl0qyImNvhlohdOf2GT1O4HQ1L1ibLWNa7tB2XQVes_glot-hNyYFUd8XQ3j8nb_d18-pjOnh-eprezVGclbdMKFBeVyrJsUlkwQgmhGGVZxSslSsjRIGfccMgnRhVCcC14CYUqSsqUyHl2TM63d1fBf3cYW7l0UWNdqwZ9F-UEgBciywdjsTXq4GMMaOUquKUKvQQq1zTlhqZco5Ic5IamZEPubFfQVUs0f6kdvkG_2eo4fPnjMMioHTYajQuoW2m8-6fhF1xbhUk</recordid><startdate>19710806</startdate><enddate>19710806</enddate><creator>Kaufman, Bernard T.</creator><creator>Pierce, Jack V.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19710806</creationdate><title>Purification of dihydrofolic reductase from chicken liver by affinity chromatography</title><author>Kaufman, Bernard T. ; Pierce, Jack V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-b1a79ba3338bf1d9a99a2023b7ba9614ede727d7148da5997c97615a5602a9473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1971</creationdate><topic>Ammonium Sulfate</topic><topic>Animals</topic><topic>Chemical Phenomena</topic><topic>Chemical Precipitation</topic><topic>Chemistry</topic><topic>Chickens</topic><topic>Chromatography</topic><topic>Chromatography, Gel</topic><topic>Cyanides</topic><topic>Folic Acid</topic><topic>Hydroxyapatites</topic><topic>Imides</topic><topic>Liver - enzymology</topic><topic>Methods</topic><topic>Methotrexate</topic><topic>Methylamines</topic><topic>Polyamines</topic><topic>Polysaccharides</topic><topic>Protein Binding</topic><topic>Tetrahydrofolate Dehydrogenase - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kaufman, Bernard T.</creatorcontrib><creatorcontrib>Pierce, Jack V.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kaufman, Bernard T.</au><au>Pierce, Jack V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of dihydrofolic reductase from chicken liver by affinity chromatography</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1971-08-06</date><risdate>1971</risdate><volume>44</volume><issue>3</issue><spage>608</spage><epage>613</epage><pages>608-613</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The procedure for coupling methotrexate (4-amino-10-methylpteroylglutamic acid) to Sepharose via a six carbon chain is described. An affinity column prepared from this material quantitatively adsorbs the dihydrofolic reductase activity from a partially purified extract of chicken liver. Elution of the enzyme readily occurs with dilute K
2HPO
4 in the presence of dihydrofolate. Approximately 250-fold purification occurs by affinity chromatography yielding a preparation which appears to be homogeneous.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>5123199</pmid><doi>10.1016/S0006-291X(71)80126-2</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1971-08, Vol.44 (3), p.608-613 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81175934 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Ammonium Sulfate Animals Chemical Phenomena Chemical Precipitation Chemistry Chickens Chromatography Chromatography, Gel Cyanides Folic Acid Hydroxyapatites Imides Liver - enzymology Methods Methotrexate Methylamines Polyamines Polysaccharides Protein Binding Tetrahydrofolate Dehydrogenase - isolation & purification |
| title | Purification of dihydrofolic reductase from chicken liver by affinity chromatography |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T15%3A09%3A16IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20of%20dihydrofolic%20reductase%20from%20chicken%20liver%20by%20affinity%20chromatography&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Kaufman,%20Bernard%20T.&rft.date=1971-08-06&rft.volume=44&rft.issue=3&rft.spage=608&rft.epage=613&rft.pages=608-613&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/S0006-291X(71)80126-2&rft_dat=%3Cproquest_cross%3E81175934%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=81175934&rft_id=info:pmid/5123199&rft_els_id=S0006291X71801262&rfr_iscdi=true |