Circular dichroism changes in galactosyltransferase upon substrate binding
Circular dichroism studies with the galactosyltransferase isolated from bovine skim milk are described. Addition of UDP-galactose to the galactosyltransferase-Mn-2+ complex causes a decrease in the negative mean residue ellipticity in the 205-220-nm range and positive increases in the 265- and 275-2...
Gespeichert in:
| Veröffentlicht in: | Biochemistry (Easton) 1975-04, Vol.14 (7), p.1461-1463 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1463 |
|---|---|
| container_issue | 7 |
| container_start_page | 1461 |
| container_title | Biochemistry (Easton) |
| container_volume | 14 |
| creator | Geren, Collis R Magee, Steve C Ebner, Kurt E |
| description | Circular dichroism studies with the galactosyltransferase isolated from bovine skim milk are described. Addition of UDP-galactose to the galactosyltransferase-Mn-2+ complex causes a decrease in the negative mean residue ellipticity in the 205-220-nm range and positive increases in the 265- and 275-290-nm ellipticity. These date are consistent with the view that a conformation change involving aromatic amino acid residues occurs upon the binding of UDP-galactose to the galactosyltransferase-Mn-2+ complex. No effects in the near-ultraviolet circular dichroism spectrum were observed upon the addition of UDP or glucose to the galactosyltransferase-Mn-2+ complex. |
| doi_str_mv | 10.1021/bi00678a017 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_82839362</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>82839362</sourcerecordid><originalsourceid>FETCH-LOGICAL-a354t-2c04692df0c5e5d53d64b1672e33eb91bd7706d627e23d4f777202d74e0975943</originalsourceid><addsrcrecordid>eNptkEtLxDAURoMoOj5WroWudCHVvNMuZdRRGVF8rEOapGPGTjvmtuD8eysd1IWry73n8F34EDok-IxgSs6LgLFUmcFEbaARERSnPM_FJhrhHqQ0l3gH7QLM-5VjxbfRNiFUkIyO0N04RNtVJiYu2LfYBFgk9s3UMw9JqJOZqYxtG1hVbTQ1lD4a8Em3bOoEugL6Y-uTItQu1LN9tFWaCvzBeu6h1-url_FNOn2Y3I4vpqlhgrcptZjLnLoSW-GFE8xJXhCpqGfMFzkpnFJYOkmVp8zxUilFMXWKe5wrkXO2h46H3GVsPjoPrV4EsL6qTO2bDnRGM5YzSXvxdBBtbACiL_UyhoWJK02w_m5O_2mut4_WsV2x8O7XHarqeTrwAK3__MEmvmupmBL65fFZT-i9eMouJ5r0_sngGwt63nSx7kv59_MXRZOD6w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82839362</pqid></control><display><type>article</type><title>Circular dichroism changes in galactosyltransferase upon substrate binding</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Geren, Collis R ; Magee, Steve C ; Ebner, Kurt E</creator><creatorcontrib>Geren, Collis R ; Magee, Steve C ; Ebner, Kurt E</creatorcontrib><description>Circular dichroism studies with the galactosyltransferase isolated from bovine skim milk are described. Addition of UDP-galactose to the galactosyltransferase-Mn-2+ complex causes a decrease in the negative mean residue ellipticity in the 205-220-nm range and positive increases in the 265- and 275-290-nm ellipticity. These date are consistent with the view that a conformation change involving aromatic amino acid residues occurs upon the binding of UDP-galactose to the galactosyltransferase-Mn-2+ complex. No effects in the near-ultraviolet circular dichroism spectrum were observed upon the addition of UDP or glucose to the galactosyltransferase-Mn-2+ complex.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00678a017</identifier><identifier>PMID: 1125182</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Binding Sites ; Cattle ; Circular Dichroism ; Female ; Galactose ; Hexosyltransferases - metabolism ; Kinetics ; Manganese ; Milk - enzymology ; Protein Binding ; Protein Conformation ; Spectrophotometry, Ultraviolet ; Uridine Diphosphate Sugars</subject><ispartof>Biochemistry (Easton), 1975-04, Vol.14 (7), p.1461-1463</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a354t-2c04692df0c5e5d53d64b1672e33eb91bd7706d627e23d4f777202d74e0975943</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00678a017$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00678a017$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1125182$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Geren, Collis R</creatorcontrib><creatorcontrib>Magee, Steve C</creatorcontrib><creatorcontrib>Ebner, Kurt E</creatorcontrib><title>Circular dichroism changes in galactosyltransferase upon substrate binding</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Circular dichroism studies with the galactosyltransferase isolated from bovine skim milk are described. Addition of UDP-galactose to the galactosyltransferase-Mn-2+ complex causes a decrease in the negative mean residue ellipticity in the 205-220-nm range and positive increases in the 265- and 275-290-nm ellipticity. These date are consistent with the view that a conformation change involving aromatic amino acid residues occurs upon the binding of UDP-galactose to the galactosyltransferase-Mn-2+ complex. No effects in the near-ultraviolet circular dichroism spectrum were observed upon the addition of UDP or glucose to the galactosyltransferase-Mn-2+ complex.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Cattle</subject><subject>Circular Dichroism</subject><subject>Female</subject><subject>Galactose</subject><subject>Hexosyltransferases - metabolism</subject><subject>Kinetics</subject><subject>Manganese</subject><subject>Milk - enzymology</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Uridine Diphosphate Sugars</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkEtLxDAURoMoOj5WroWudCHVvNMuZdRRGVF8rEOapGPGTjvmtuD8eysd1IWry73n8F34EDok-IxgSs6LgLFUmcFEbaARERSnPM_FJhrhHqQ0l3gH7QLM-5VjxbfRNiFUkIyO0N04RNtVJiYu2LfYBFgk9s3UMw9JqJOZqYxtG1hVbTQ1lD4a8Em3bOoEugL6Y-uTItQu1LN9tFWaCvzBeu6h1-url_FNOn2Y3I4vpqlhgrcptZjLnLoSW-GFE8xJXhCpqGfMFzkpnFJYOkmVp8zxUilFMXWKe5wrkXO2h46H3GVsPjoPrV4EsL6qTO2bDnRGM5YzSXvxdBBtbACiL_UyhoWJK02w_m5O_2mut4_WsV2x8O7XHarqeTrwAK3__MEmvmupmBL65fFZT-i9eMouJ5r0_sngGwt63nSx7kv59_MXRZOD6w</recordid><startdate>19750401</startdate><enddate>19750401</enddate><creator>Geren, Collis R</creator><creator>Magee, Steve C</creator><creator>Ebner, Kurt E</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>19750401</creationdate><title>Circular dichroism changes in galactosyltransferase upon substrate binding</title><author>Geren, Collis R ; Magee, Steve C ; Ebner, Kurt E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a354t-2c04692df0c5e5d53d64b1672e33eb91bd7706d627e23d4f777202d74e0975943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Cattle</topic><topic>Circular Dichroism</topic><topic>Female</topic><topic>Galactose</topic><topic>Hexosyltransferases - metabolism</topic><topic>Kinetics</topic><topic>Manganese</topic><topic>Milk - enzymology</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Uridine Diphosphate Sugars</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Geren, Collis R</creatorcontrib><creatorcontrib>Magee, Steve C</creatorcontrib><creatorcontrib>Ebner, Kurt E</creatorcontrib><collection>Istex</collection><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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Geren, Collis R</au><au>Magee, Steve C</au><au>Ebner, Kurt E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Circular dichroism changes in galactosyltransferase upon substrate binding</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1975-04-01</date><risdate>1975</risdate><volume>14</volume><issue>7</issue><spage>1461</spage><epage>1463</epage><pages>1461-1463</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Circular dichroism studies with the galactosyltransferase isolated from bovine skim milk are described. Addition of UDP-galactose to the galactosyltransferase-Mn-2+ complex causes a decrease in the negative mean residue ellipticity in the 205-220-nm range and positive increases in the 265- and 275-290-nm ellipticity. These date are consistent with the view that a conformation change involving aromatic amino acid residues occurs upon the binding of UDP-galactose to the galactosyltransferase-Mn-2+ complex. No effects in the near-ultraviolet circular dichroism spectrum were observed upon the addition of UDP or glucose to the galactosyltransferase-Mn-2+ complex.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>1125182</pmid><doi>10.1021/bi00678a017</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 1975-04, Vol.14 (7), p.1461-1463 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82839362 |
| source | MEDLINE; American Chemical Society Journals |
| subjects | Animals Binding Sites Cattle Circular Dichroism Female Galactose Hexosyltransferases - metabolism Kinetics Manganese Milk - enzymology Protein Binding Protein Conformation Spectrophotometry, Ultraviolet Uridine Diphosphate Sugars |
| title | Circular dichroism changes in galactosyltransferase upon substrate binding |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T11%3A54%3A11IST&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=Circular%20dichroism%20changes%20in%20galactosyltransferase%20upon%20substrate%20binding&rft.jtitle=Biochemistry%20(Easton)&rft.au=Geren,%20Collis%20R&rft.date=1975-04-01&rft.volume=14&rft.issue=7&rft.spage=1461&rft.epage=1463&rft.pages=1461-1463&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00678a017&rft_dat=%3Cproquest_cross%3E82839362%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=82839362&rft_id=info:pmid/1125182&rfr_iscdi=true |