Fixation of aldehydic dextrans onto human deoxyhemoglobin.
Identifieur interne : 000259 ( PubMed/Corpus ); précédent : 000258; suivant : 000260Fixation of aldehydic dextrans onto human deoxyhemoglobin.
Auteurs : D. Klett ; M. Grandgeorge ; E. DellacherieSource :
- Biopolymers [ 0006-3525 ] ; 1992.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Aldehydes, Dextrans, Hemoglobin A, Oxyhemoglobins.
- chemical , pharmacology : Phytic Acid.
- Humans, Protein Binding.
Abstract
A procedure commonly used to transform native adult human hemoglobin (Hb) into a physiological oxygen carrier consists of a pyridoxylation of the protein to lower its oxygen affinity, followed by its polymerization in the presence of glutaraldehyde, with or without further reduction, to increase its circulating half-life. This series of reactions yields derivatives presenting a great molecular heterogeneity that have to be fractionated for use in vivo. Hemoglobin derivatives with low oxygen affinity and a narrow distribution of molecular weights were obtained by linking a dextran polyaldehydic derivative to deoxyhemoglobin at pH 8. From oxygen-binding measurements carried out in the presence of inositolhexaphosphate, a strong effector of hemoglobin, it appeared that the allosteric site of hemoglobin was blocked, probably by crosslinking bonds, which stabilizes its deoxy structure. On the other hand, when the reaction was performed in the presence of inositolhexaphosphate, the resulting conjugates exhibited an oxygen affinity identical to that of unmodified hemoglobin. After treatment with NaBH4, the polymer-hemoglobin derivatives were stable and possessed a reversible oxygen-carrying capacity similar to that of blood. The conjugates prepared from oxyhemoglobin all possessed a lower P50 than native hemoglobin whatever the reaction conditions.
DOI: 10.1002/bip.360320507
PubMed: 1381226
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pubmed:1381226Le document en format XML
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Dellacherie</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1992">1992</date><idno type="RBID">pubmed:1381226</idno><idno type="pmid">1381226</idno><idno type="doi">10.1002/bip.360320507</idno><idno type="wicri:Area/PubMed/Corpus">000259</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000259</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Fixation of aldehydic dextrans onto human deoxyhemoglobin.</title><author><name sortKey="Klett, D" sort="Klett, D" uniqKey="Klett D" first="D" last="Klett">D. Klett</name><affiliation><nlm:affiliation>Laboratoire de Chimie-Physique Macromoléculaire, URA CNRS 494, ENSIC, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Grandgeorge, M" sort="Grandgeorge, M" uniqKey="Grandgeorge M" first="M" last="Grandgeorge">M. Grandgeorge</name></author><author><name sortKey="Dellacherie, E" sort="Dellacherie, E" uniqKey="Dellacherie E" first="E" last="Dellacherie">E. Dellacherie</name></author></analytic><series><title level="j">Biopolymers</title><idno type="ISSN">0006-3525</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldehydes (metabolism)</term><term>Dextrans (metabolism)</term><term>Hemoglobin A (metabolism)</term><term>Humans</term><term>Oxyhemoglobins (metabolism)</term><term>Phytic Acid (pharmacology)</term><term>Protein Binding</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aldehydes</term><term>Dextrans</term><term>Hemoglobin A</term><term>Oxyhemoglobins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Phytic Acid</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Protein Binding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A procedure commonly used to transform native adult human hemoglobin (Hb) into a physiological oxygen carrier consists of a pyridoxylation of the protein to lower its oxygen affinity, followed by its polymerization in the presence of glutaraldehyde, with or without further reduction, to increase its circulating half-life. This series of reactions yields derivatives presenting a great molecular heterogeneity that have to be fractionated for use in vivo. Hemoglobin derivatives with low oxygen affinity and a narrow distribution of molecular weights were obtained by linking a dextran polyaldehydic derivative to deoxyhemoglobin at pH 8. From oxygen-binding measurements carried out in the presence of inositolhexaphosphate, a strong effector of hemoglobin, it appeared that the allosteric site of hemoglobin was blocked, probably by crosslinking bonds, which stabilizes its deoxy structure. On the other hand, when the reaction was performed in the presence of inositolhexaphosphate, the resulting conjugates exhibited an oxygen affinity identical to that of unmodified hemoglobin. After treatment with NaBH4, the polymer-hemoglobin derivatives were stable and possessed a reversible oxygen-carrying capacity similar to that of blood. The conjugates prepared from oxyhemoglobin all possessed a lower P50 than native hemoglobin whatever the reaction conditions.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">1381226</PMID><DateCreated><Year>1992</Year><Month>10</Month><Day>07</Day></DateCreated><DateCompleted><Year>1992</Year><Month>10</Month><Day>07</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3525</ISSN><JournalIssue CitedMedium="Print"><Volume>32</Volume><Issue>5</Issue><PubDate><Year>1992</Year><Month>May</Month></PubDate></JournalIssue><Title>Biopolymers</Title><ISOAbbreviation>Biopolymers</ISOAbbreviation></Journal><ArticleTitle>Fixation of aldehydic dextrans onto human deoxyhemoglobin.</ArticleTitle><Pagination><MedlinePgn>517-22</MedlinePgn></Pagination><Abstract><AbstractText>A procedure commonly used to transform native adult human hemoglobin (Hb) into a physiological oxygen carrier consists of a pyridoxylation of the protein to lower its oxygen affinity, followed by its polymerization in the presence of glutaraldehyde, with or without further reduction, to increase its circulating half-life. This series of reactions yields derivatives presenting a great molecular heterogeneity that have to be fractionated for use in vivo. Hemoglobin derivatives with low oxygen affinity and a narrow distribution of molecular weights were obtained by linking a dextran polyaldehydic derivative to deoxyhemoglobin at pH 8. From oxygen-binding measurements carried out in the presence of inositolhexaphosphate, a strong effector of hemoglobin, it appeared that the allosteric site of hemoglobin was blocked, probably by crosslinking bonds, which stabilizes its deoxy structure. On the other hand, when the reaction was performed in the presence of inositolhexaphosphate, the resulting conjugates exhibited an oxygen affinity identical to that of unmodified hemoglobin. After treatment with NaBH4, the polymer-hemoglobin derivatives were stable and possessed a reversible oxygen-carrying capacity similar to that of blood. The conjugates prepared from oxyhemoglobin all possessed a lower P50 than native hemoglobin whatever the reaction conditions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Klett</LastName><ForeName>D</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Laboratoire de Chimie-Physique Macromoléculaire, URA CNRS 494, ENSIC, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grandgeorge</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Dellacherie</LastName><ForeName>E</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>UNITED STATES</Country><MedlineTA>Biopolymers</MedlineTA><NlmUniqueID>0372525</NlmUniqueID><ISSNLinking>0006-3525</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000447">Aldehydes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010108">Oxyhemoglobins</NameOfSubstance></Chemical><Chemical><RegistryNumber>7IGF0S7R8I</RegistryNumber><NameOfSubstance UI="D010833">Phytic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>9034-51-9</RegistryNumber><NameOfSubstance UI="D006441">Hemoglobin A</NameOfSubstance></Chemical><Chemical><RegistryNumber>9062-91-3</RegistryNumber><NameOfSubstance UI="C029774">oxyhemoglobin A</NameOfSubstance></Chemical><Chemical><RegistryNumber>K3R6ZDH4DU</RegistryNumber><NameOfSubstance UI="D003911">Dextrans</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D000447">Aldehydes</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D003911">Dextrans</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D006441">Hemoglobin A</DescriptorName><QualifierName MajorTopicYN="Y" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D006801">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D010108">Oxyhemoglobins</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000378">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D010833">Phytic Acid</DescriptorName><QualifierName MajorTopicYN="N" UI="Q000494">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N" UI="D011485">Protein Binding</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>5</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1381226</ArticleId><ArticleId IdType="doi">10.1002/bip.360320507</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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