Improvement of oxygen-carrying properties of human hemoglobin by chemical modification with a benzene hexacarboxylate-monosubstituted polyoxyethylene
Identifieur interne : 000965 ( Istex/Corpus ); précédent : 000964; suivant : 000966Improvement of oxygen-carrying properties of human hemoglobin by chemical modification with a benzene hexacarboxylate-monosubstituted polyoxyethylene
Auteurs : Edith Dellacherie ; Michèle LéonardSource :
- Journal of Protein Chemistry [ 0277-8033 ] ; 1991-02-01.
English descriptors
- KwdEn :
- Allosteric site, Amino groups, Biological membranes, Blood substitutes, Chemical modification, Conjugate, Covalent, Covalent conjugates, Covalent fixation, Dellacherie, Deoxyhb, Edci, Filtration elution profiles, Fixation, Flow rate, Globin, Human hemoglobin, Inositol hexaphosphate, L6onard, Molar, Molar ratio, Oxygen affinity, Oxyhb, Peptide, Peptide maps, Polymeric reagent, Pyridoxal phosphate, Reaction conditions, Reagent, Relative amount, Site specificity, Tryptic, Tryptic maps.
- Teeft :
- Allosteric site, Amino groups, Biological membranes, Blood substitutes, Chemical modification, Conjugate, Covalent, Covalent conjugates, Covalent fixation, Dellacherie, Deoxyhb, Edci, Filtration elution profiles, Fixation, Flow rate, Globin, Human hemoglobin, Inositol hexaphosphate, L6onard, Molar, Molar ratio, Oxygen affinity, Oxyhb, Peptide, Peptide maps, Polymeric reagent, Pyridoxal phosphate, Reaction conditions, Reagent, Relative amount, Site specificity, Tryptic, Tryptic maps.
Abstract
Abstract: Benzene hexacarboxylate-monosubstituted polyoxyethylene on contact with Hb decreases its oxygen affinity, probably because it specifically interacts with the amino groups of the phosphate-binding site. This site specificity was used to direct the covalent coupling of this polymeric reagent with hemoglobin, in the vicinity of this β cleft in order to obtain conjugates with low oxygen affinity and well-defined molecular weight. Such conjugates could thus be regarded as potential candidates for blood substitutes. Covalent fixation of this polymeric site-labeling reagent onto hemoglobin was carried out with the oxy and the deoxy form in the presence of a water soluble carbodiimide. It turns out that the oxygen-binding properties of the resulting hemoglobin derivatives depend on the reaction conditions, yet in all cases the oxygen affinity of the modified protein was lower than that of native hemoglobin and was no longer affected by organic phosphates. These results indicate that phosphate-binding site amines are probably involved in the covalent coupling, although in some conjugates (especially those prepared with high ratios of reagents) other amino groups participate also in the linking to the polymer. Chromatographic analysis and trypic peptide mapping of some conjugates evidenced that the β-terminal valine residue was in fact the preferential binding site of hexacarboxylate-monosubstituted polyoxyethylene.
Url:
DOI: 10.1007/BF01024656
Links to Exploration step
ISTEX:2F8F34E2C023127EF5927A5B13DB2ECEF283EBE1Le document en format XML
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This site specificity was used to direct the covalent coupling of this polymeric reagent with hemoglobin, in the vicinity of this β cleft in order to obtain conjugates with low oxygen affinity and well-defined molecular weight. Such conjugates could thus be regarded as potential candidates for blood substitutes. Covalent fixation of this polymeric site-labeling reagent onto hemoglobin was carried out with the oxy and the deoxy form in the presence of a water soluble carbodiimide. It turns out that the oxygen-binding properties of the resulting hemoglobin derivatives depend on the reaction conditions, yet in all cases the oxygen affinity of the modified protein was lower than that of native hemoglobin and was no longer affected by organic phosphates. These results indicate that phosphate-binding site amines are probably involved in the covalent coupling, although in some conjugates (especially those prepared with high ratios of reagents) other amino groups participate also in the linking to the polymer. Chromatographic analysis and trypic peptide mapping of some conjugates evidenced that the β-terminal valine residue was in fact the preferential binding site of hexacarboxylate-monosubstituted polyoxyethylene.</div></front></TEI><istex><corpusName>springer</corpusName><keywords><teeft><json:string>globin</json:string><json:string>l6onard</json:string><json:string>dellacherie</json:string><json:string>edci</json:string><json:string>oxyhb</json:string><json:string>tryptic</json:string><json:string>deoxyhb</json:string><json:string>covalent</json:string><json:string>molar ratio</json:string><json:string>oxygen affinity</json:string><json:string>fixation</json:string><json:string>flow rate</json:string><json:string>allosteric site</json:string><json:string>molar</json:string><json:string>peptide</json:string><json:string>reagent</json:string><json:string>covalent fixation</json:string><json:string>reaction conditions</json:string><json:string>covalent conjugates</json:string><json:string>human hemoglobin</json:string><json:string>tryptic maps</json:string><json:string>conjugate</json:string><json:string>site specificity</json:string><json:string>blood substitutes</json:string><json:string>chemical modification</json:string><json:string>pyridoxal phosphate</json:string><json:string>peptide maps</json:string><json:string>relative amount</json:string><json:string>inositol hexaphosphate</json:string><json:string>amino groups</json:string><json:string>filtration elution profiles</json:string><json:string>polymeric reagent</json:string><json:string>biological membranes</json:string></teeft></keywords><author><json:item><name>Edith Dellacherie</name><affiliations><json:string>Laboratory of Macromolecular Physical Chemistry, URA CNRS 494, ENSIC, 1 rue Grandville, BP 451, 54001, Nancy Cedex, France</json:string></affiliations></json:item><json:item><name>Michèle Léonard</name><affiliations><json:string>Laboratory of Macromolecular Physical Chemistry, URA CNRS 494, ENSIC, 1 rue Grandville, BP 451, 54001, Nancy Cedex, France</json:string></affiliations></json:item></author><articleId><json:string>BF01024656</json:string><json:string>Art8</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: Benzene hexacarboxylate-monosubstituted polyoxyethylene on contact with Hb decreases its oxygen affinity, probably because it specifically interacts with the amino groups of the phosphate-binding site. This site specificity was used to direct the covalent coupling of this polymeric reagent with hemoglobin, in the vicinity of this β cleft in order to obtain conjugates with low oxygen affinity and well-defined molecular weight. Such conjugates could thus be regarded as potential candidates for blood substitutes. Covalent fixation of this polymeric site-labeling reagent onto hemoglobin was carried out with the oxy and the deoxy form in the presence of a water soluble carbodiimide. It turns out that the oxygen-binding properties of the resulting hemoglobin derivatives depend on the reaction conditions, yet in all cases the oxygen affinity of the modified protein was lower than that of native hemoglobin and was no longer affected by organic phosphates. These results indicate that phosphate-binding site amines are probably involved in the covalent coupling, although in some conjugates (especially those prepared with high ratios of reagents) other amino groups participate also in the linking to the polymer. 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of oxygen-carrying properties of human hemoglobin by chemical modification with a benzene hexacarboxylate-monosubstituted polyoxyethylene</title><author xml:id="author-0000"><persName><forename type="first">Edith</forename><surname>Dellacherie</surname></persName><affiliation>Laboratory of Macromolecular Physical Chemistry, URA CNRS 494, ENSIC, 1 rue Grandville, BP 451, 54001, Nancy Cedex, France</affiliation></author><author xml:id="author-0001" corresp="yes"><persName><forename type="first">Michèle</forename><surname>Léonard</surname></persName><affiliation>Laboratory of Macromolecular Physical Chemistry, URA CNRS 494, ENSIC, 1 rue Grandville, BP 451, 54001, Nancy Cedex, France</affiliation></author><idno type="istex">2F8F34E2C023127EF5927A5B13DB2ECEF283EBE1</idno><idno type="ark">ark:/67375/1BB-HB67HVRS-P</idno><idno type="DOI">10.1007/BF01024656</idno><idno type="article-id">BF01024656</idno><idno type="article-id">Art8</idno></analytic><monogr><title level="j">Journal of Protein Chemistry</title><title level="j" type="abbrev">J Protein Chem</title><idno type="pISSN">0277-8033</idno><idno type="eISSN">1573-4943</idno><idno type="journal-ID">true</idno><idno type="issue-article-count">15</idno><idno type="volume-issue-count">6</idno><imprint><publisher>Kluwer Academic Publishers-Plenum Publishers</publisher><pubPlace>New York</pubPlace><date type="published" when="1991-02-01"></date><biblScope unit="volume">10</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="61">61</biblScope><biblScope unit="page" to="67">67</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1990-10-11</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Benzene hexacarboxylate-monosubstituted polyoxyethylene on contact with Hb decreases its oxygen affinity, probably because it specifically interacts with the amino groups of the phosphate-binding site. This site specificity was used to direct the covalent coupling of this polymeric reagent with hemoglobin, in the vicinity of this β cleft in order to obtain conjugates with low oxygen affinity and well-defined molecular weight. Such conjugates could thus be regarded as potential candidates for blood substitutes. Covalent fixation of this polymeric site-labeling reagent onto hemoglobin was carried out with the oxy and the deoxy form in the presence of a water soluble carbodiimide. It turns out that the oxygen-binding properties of the resulting hemoglobin derivatives depend on the reaction conditions, yet in all cases the oxygen affinity of the modified protein was lower than that of native hemoglobin and was no longer affected by organic phosphates. These results indicate that phosphate-binding site amines are probably involved in the covalent coupling, although in some conjugates (especially those prepared with high ratios of reagents) other amino groups participate also in the linking to the polymer. Chromatographic analysis and trypic peptide mapping of some conjugates evidenced that the β-terminal valine residue was in fact the preferential binding site of hexacarboxylate-monosubstituted polyoxyethylene.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>Chemistry</head><item><term>Organic Chemistry</term></item><item><term>Bioorganic Chemistry</term></item><item><term>Biochemistry, general</term></item><item><term>Animal Anatomy / Morphology / Histology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1990-10-11">Created</change><change when="1991-02-01">Published</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2017-10-3">References 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NumberingStyle="Unnumbered"><JournalID>10930</JournalID><JournalPrintISSN>0277-8033</JournalPrintISSN><JournalElectronicISSN>1573-4943</JournalElectronicISSN><JournalTitle>Journal of Protein Chemistry</JournalTitle><JournalAbbreviatedTitle>J Protein Chem</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Chemistry</JournalSubject><JournalSubject Type="Secondary">Organic Chemistry</JournalSubject><JournalSubject Type="Secondary">Bioorganic Chemistry</JournalSubject><JournalSubject Type="Secondary">Biochemistry, general</JournalSubject><JournalSubject Type="Secondary">Animal Anatomy / Morphology / Histology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>10</VolumeIDStart><VolumeIDEnd>10</VolumeIDEnd><VolumeIssueCount>6</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>1</IssueIDStart><IssueIDEnd>1</IssueIDEnd><IssueArticleCount>15</IssueArticleCount><IssueHistory><CoverDate><Year>1991</Year><Month>2</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Plenum Publishing Corporation</CopyrightHolderName><CopyrightYear>1991</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art8"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF01024656</ArticleID><ArticleDOI>10.1007/BF01024656</ArticleDOI><ArticleSequenceNumber>8</ArticleSequenceNumber><ArticleTitle Language="En">Improvement of oxygen-carrying properties of human hemoglobin by chemical modification with a benzene hexacarboxylate-monosubstituted polyoxyethylene</ArticleTitle><ArticleFirstPage>61</ArticleFirstPage><ArticleLastPage>67</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2005</Year><Month>1</Month><Day>7</Day></RegistrationDate><Received><Year>1990</Year><Month>10</Month><Day>11</Day></Received></ArticleHistory><ArticleCopyright><CopyrightHolderName>Plenum Publishing Corporation</CopyrightHolderName><CopyrightYear>1991</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>10930</JournalID><VolumeIDStart>10</VolumeIDStart><VolumeIDEnd>10</VolumeIDEnd><IssueIDStart>1</IssueIDStart><IssueIDEnd>1</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Edith</GivenName><FamilyName>Dellacherie</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Michèle</GivenName><FamilyName>Léonard</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Laboratory of Macromolecular Physical Chemistry</OrgDivision><OrgName>URA CNRS 494, ENSIC</OrgName><OrgAddress><Street>1 rue Grandville</Street><Postbox>BP 451</Postbox><Postcode>54001</Postcode><City>Nancy Cedex</City><Country>France</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>Benzene hexacarboxylate-monosubstituted polyoxyethylene on contact with Hb decreases its oxygen affinity, probably because it specifically interacts with the amino groups of the phosphate-binding site. This site specificity was used to direct the covalent coupling of this polymeric reagent with hemoglobin, in the vicinity of this β cleft in order to obtain conjugates with low oxygen affinity and well-defined molecular weight. Such conjugates could thus be regarded as potential candidates for blood substitutes. Covalent fixation of this polymeric site-labeling reagent onto hemoglobin was carried out with the oxy and the deoxy form in the presence of a water soluble carbodiimide. It turns out that the oxygen-binding properties of the resulting hemoglobin derivatives depend on the reaction conditions, yet in all cases the oxygen affinity of the modified protein was lower than that of native hemoglobin and was no longer affected by organic phosphates. These results indicate that phosphate-binding site amines are probably involved in the covalent coupling, although in some conjugates (especially those prepared with high ratios of reagents) other amino groups participate also in the linking to the polymer. Chromatographic analysis and trypic peptide mapping of some conjugates evidenced that the β-terminal valine residue was in fact the preferential binding site of hexacarboxylate-monosubstituted polyoxyethylene.</Para></Abstract><KeywordGroup Language="En"><Heading>Key words</Heading><Keyword>Hemoglobin</Keyword><Keyword>polyoxyethylene</Keyword><Keyword>site-labeling reagent</Keyword><Keyword>low oxygen affinity</Keyword><Keyword>blood substitute</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Improvement of oxygen-carrying properties of human hemoglobin by chemical modification with a benzene hexacarboxylate-monosubstituted polyoxyethylene</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Improvement of oxygen-carrying properties of human hemoglobin by chemical modification with a benzene hexacarboxylate-monosubstituted polyoxyethylene</title></titleInfo><name type="personal"><namePart type="given">Edith</namePart><namePart type="family">Dellacherie</namePart><affiliation>Laboratory of Macromolecular Physical Chemistry, URA CNRS 494, ENSIC, 1 rue Grandville, BP 451, 54001, Nancy Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">Michèle</namePart><namePart type="family">Léonard</namePart><affiliation>Laboratory of Macromolecular Physical Chemistry, URA CNRS 494, ENSIC, 1 rue Grandville, BP 451, 54001, Nancy Cedex, France</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><dateCreated encoding="w3cdtf">1990-10-11</dateCreated><dateIssued encoding="w3cdtf">1991-02-01</dateIssued><dateIssued encoding="w3cdtf">1991</dateIssued><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Benzene hexacarboxylate-monosubstituted polyoxyethylene on contact with Hb decreases its oxygen affinity, probably because it specifically interacts with the amino groups of the phosphate-binding site. This site specificity was used to direct the covalent coupling of this polymeric reagent with hemoglobin, in the vicinity of this β cleft in order to obtain conjugates with low oxygen affinity and well-defined molecular weight. Such conjugates could thus be regarded as potential candidates for blood substitutes. Covalent fixation of this polymeric site-labeling reagent onto hemoglobin was carried out with the oxy and the deoxy form in the presence of a water soluble carbodiimide. It turns out that the oxygen-binding properties of the resulting hemoglobin derivatives depend on the reaction conditions, yet in all cases the oxygen affinity of the modified protein was lower than that of native hemoglobin and was no longer affected by organic phosphates. These results indicate that phosphate-binding site amines are probably involved in the covalent coupling, although in some conjugates (especially those prepared with high ratios of reagents) other amino groups participate also in the linking to the polymer. Chromatographic analysis and trypic peptide mapping of some conjugates evidenced that the β-terminal valine residue was in fact the preferential binding site of hexacarboxylate-monosubstituted polyoxyethylene.</abstract><relatedItem type="host"><titleInfo><title>Journal of Protein Chemistry</title></titleInfo><titleInfo type="abbreviated"><title>J Protein Chem</title></titleInfo><genre type="journal" displayLabel="Archive Journal" authority="ISTEX" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">1991-02-01</dateIssued><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><subject><genre>Chemistry</genre><topic>Organic Chemistry</topic><topic>Bioorganic Chemistry</topic><topic>Biochemistry, general</topic><topic>Animal Anatomy / Morphology / Histology</topic></subject><identifier type="ISSN">0277-8033</identifier><identifier type="eISSN">1573-4943</identifier><identifier type="JournalID">10930</identifier><identifier type="IssueArticleCount">15</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>1991</date><detail type="volume"><number>10</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="pages"><start>61</start><end>67</end></extent></part><recordInfo><recordOrigin>Plenum Publishing Corporation, 1991</recordOrigin></recordInfo></relatedItem><identifier type="istex">2F8F34E2C023127EF5927A5B13DB2ECEF283EBE1</identifier><identifier type="ark">ark:/67375/1BB-HB67HVRS-P</identifier><identifier type="DOI">10.1007/BF01024656</identifier><identifier type="ArticleID">BF01024656</identifier><identifier type="ArticleID">Art8</identifier><accessCondition type="use and reproduction" contentType="copyright">Plenum Publishing Corporation, 1991</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, 1991</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/2F8F34E2C023127EF5927A5B13DB2ECEF283EBE1/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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