Investigation of surface oligonucleotide-binding proteins of eucaryotic cells by affinity modification with reactive oligonucleotide derivatives
Identifieur interne : 002021 ( Istex/Corpus ); précédent : 002020; suivant : 002022Investigation of surface oligonucleotide-binding proteins of eucaryotic cells by affinity modification with reactive oligonucleotide derivatives
Auteurs : B. P. Chelobanov ; P. P. Laktionov ; M. V. Khar Kova ; E. Yu. Rykova ; D. V. Pyshnyi ; I. A. Pyshnaya ; V. N. Silnikov ; V. V. VlassovSource :
- Russian Chemical Bulletin [ 1066-5285 ] ; 2002-07-01.
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Abstract
Abstract: Interactions between oligodeoxyribonucleotides (ODN) with different sequences and cell proteins were examined using the affinity modification by [32P]-labeled reactive oligonucleotide derivatives. 3"-Terminal ribouridine oxidized with sodium periodate, 4-[(N-2-chloroethyl-N-methyl)amino]benzylamine, and the maleimide residue were used as reactive groups. All the compounds used are specific reagents. The set of the discovered nucleic acid-binding (NA-binding) proteins depends on the chemical properties of the affinity reagent. The presence of the hydrophobic group at the 5"-terminus of the ODN molecule is the key factor determining the variety of the discovered NA-binding proteins. The cells of different origin (A431, HeLa, KB, MCF-7, Hap-2, K562, Cos-7, NIH/3T3, human-lung primary epithelial cells, and porcine kidney primary cells) are characterized by the same set of NA-binding proteins whose affinity modifications depends on the conditions of incubation of oligonucleotides with the cells. Treatments of cells disturbing the integrity of the cellular membrane (scrapping, treatment with trypsin, or cell permeabilization with streptolysin O or saponin), disrupt interactions between NA-binding proteins from native cells and ODN.
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DOI: 10.1023/A:1020992227792
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All the compounds used are specific reagents. The set of the discovered nucleic acid-binding (NA-binding) proteins depends on the chemical properties of the affinity reagent. The presence of the hydrophobic group at the 5"-terminus of the ODN molecule is the key factor determining the variety of the discovered NA-binding proteins. The cells of different origin (A431, HeLa, KB, MCF-7, Hap-2, K562, Cos-7, NIH/3T3, human-lung primary epithelial cells, and porcine kidney primary cells) are characterized by the same set of NA-binding proteins whose affinity modifications depends on the conditions of incubation of oligonucleotides with the cells. Treatments of cells disturbing the integrity of the cellular membrane (scrapping, treatment with trypsin, or cell permeabilization with streptolysin O or saponin), disrupt interactions between NA-binding proteins from native cells and ODN.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>B. P. 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All the compounds used are specific reagents. The set of the discovered nucleic acid-binding (NA-binding) proteins depends on the chemical properties of the affinity reagent. The presence of the hydrophobic group at the 5"-terminus of the ODN molecule is the key factor determining the variety of the discovered NA-binding proteins. The cells of different origin (A431, HeLa, KB, MCF-7, Hap-2, K562, Cos-7, NIH/3T3, human-lung primary epithelial cells, and porcine kidney primary cells) are characterized by the same set of NA-binding proteins whose affinity modifications depends on the conditions of incubation of oligonucleotides with the cells. 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Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>11172</JournalID><VolumeIDStart>51</VolumeIDStart><VolumeIDEnd>51</VolumeIDEnd><IssueIDStart>7</IssueIDStart><IssueIDEnd>7</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>B.</GivenName><GivenName>P.</GivenName><FamilyName>Chelobanov</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>P.</GivenName><GivenName>P.</GivenName><FamilyName>Laktionov</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>M.</GivenName><GivenName>V.</GivenName><FamilyName>Khar"kova</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>E.</GivenName><GivenName>Yu.</GivenName><FamilyName>Rykova</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>D.</GivenName><GivenName>V.</GivenName><FamilyName>Pyshnyi</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>I.</GivenName><GivenName>A.</GivenName><FamilyName>Pyshnaya</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>V.</GivenName><GivenName>N.</GivenName><FamilyName>Silnikov</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>V.</GivenName><GivenName>V.</GivenName><FamilyName>Vlassov</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgName>Novosibirsk Institute of Bioorganic Chemistry</OrgName><OrgAddress><Street>8 prosp. Akad. Lavrent"eva</Street><Postcode>630090</Postcode><City>Novosibirsk</City><Country>Russian Federation</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>Interactions between oligodeoxyribonucleotides (ODN) with different sequences and cell proteins were examined using the affinity modification by [<Superscript>32</Superscript>P]-labeled reactive oligonucleotide derivatives. 3"-Terminal ribouridine oxidized with sodium periodate, 4-[(<Emphasis Type="Italic">N</Emphasis>-2-chloroethyl-<Emphasis Type="Italic">N</Emphasis>-methyl)amino]benzylamine, and the maleimide residue were used as reactive groups. All the compounds used are specific reagents. The set of the discovered nucleic acid-binding (NA-binding) proteins depends on the chemical properties of the affinity reagent. The presence of the hydrophobic group at the 5"-terminus of the ODN molecule is the key factor determining the variety of the discovered NA-binding proteins. The cells of different origin (A431, HeLa, KB, MCF-7, Hap-2, K562, Cos-7, NIH/3T3, human-lung primary epithelial cells, and porcine kidney primary cells) are characterized by the same set of NA-binding proteins whose affinity modifications depends on the conditions of incubation of oligonucleotides with the cells. Treatments of cells disturbing the integrity of the cellular membrane (scrapping, treatment with trypsin, or cell permeabilization with streptolysin O or saponin), disrupt interactions between NA-binding proteins from native cells and ODN.</Para></Abstract><KeywordGroup Language="En"><Keyword>oligonucleotides</Keyword><Keyword>oligonucleotide-binding proteins</Keyword><Keyword>nucleic acid receptors</Keyword><Keyword>affinity modification</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Investigation of surface oligonucleotide-binding proteins of eucaryotic cells by affinity modification with reactive oligonucleotide derivatives</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Investigation of surface oligonucleotide-binding proteins of eucaryotic cells by affinity modification with reactive oligonucleotide derivatives</title></titleInfo><name type="personal"><namePart type="given">B.</namePart><namePart type="given">P.</namePart><namePart type="family">Chelobanov</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.</namePart><namePart type="given">P.</namePart><namePart type="family">Laktionov</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="given">V.</namePart><namePart type="family">Khar"kova</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">E.</namePart><namePart type="given">Yu.</namePart><namePart type="family">Rykova</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.</namePart><namePart type="given">V.</namePart><namePart type="family">Pyshnyi</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">I.</namePart><namePart type="given">A.</namePart><namePart type="family">Pyshnaya</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">V.</namePart><namePart type="given">N.</namePart><namePart type="family">Silnikov</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">V.</namePart><namePart type="given">V.</namePart><namePart type="family">Vlassov</namePart><affiliation>Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Kluwer Academic Publishers-Plenum Publishers</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2002-07-01</dateIssued><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Interactions between oligodeoxyribonucleotides (ODN) with different sequences and cell proteins were examined using the affinity modification by [32P]-labeled reactive oligonucleotide derivatives. 3"-Terminal ribouridine oxidized with sodium periodate, 4-[(N-2-chloroethyl-N-methyl)amino]benzylamine, and the maleimide residue were used as reactive groups. All the compounds used are specific reagents. The set of the discovered nucleic acid-binding (NA-binding) proteins depends on the chemical properties of the affinity reagent. The presence of the hydrophobic group at the 5"-terminus of the ODN molecule is the key factor determining the variety of the discovered NA-binding proteins. The cells of different origin (A431, HeLa, KB, MCF-7, Hap-2, K562, Cos-7, NIH/3T3, human-lung primary epithelial cells, and porcine kidney primary cells) are characterized by the same set of NA-binding proteins whose affinity modifications depends on the conditions of incubation of oligonucleotides with the cells. Treatments of cells disturbing the integrity of the cellular membrane (scrapping, treatment with trypsin, or cell permeabilization with streptolysin O or saponin), disrupt interactions between NA-binding proteins from native cells and ODN.</abstract><subject lang="en"><topic>oligonucleotides</topic><topic>oligonucleotide-binding proteins</topic><topic>nucleic acid receptors</topic><topic>affinity modification</topic></subject><relatedItem type="host"><titleInfo><title>Russian Chemical Bulletin</title></titleInfo><titleInfo type="abbreviated"><title>Russian Chemical Bulletin</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2002-07-01</dateIssued><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><subject><genre>Chemistry</genre><topic>Chemistry/Food Science, general</topic></subject><identifier type="ISSN">1066-5285</identifier><identifier type="eISSN">1573-9171</identifier><identifier type="JournalID">11172</identifier><identifier type="IssueArticleCount">36</identifier><identifier type="VolumeIssueCount">12</identifier><part><date>2002</date><detail type="volume"><number>51</number><caption>vol.</caption></detail><detail type="issue"><number>7</number><caption>no.</caption></detail><extent unit="pages"><start>1204</start><end>1211</end></extent></part><recordInfo><recordOrigin>Plenum Publishing Corporation, 2002</recordOrigin></recordInfo></relatedItem><identifier type="istex">388EA8F4DC3B0BF6F8635B0EF5A76BAF14F65AFE</identifier><identifier type="ark">ark:/67375/VQC-3D5FDC47-0</identifier><identifier type="DOI">10.1023/A:1020992227792</identifier><identifier type="ArticleID">456340</identifier><identifier type="ArticleID">Art16</identifier><accessCondition type="use and reproduction" contentType="copyright">Plenum Publishing Corporation, 2002</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Plenum Publishing Corporation, 2002</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-3D5FDC47-0/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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