Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability
Identifieur interne : 000856 ( Istex/Curation ); précédent : 000855; suivant : 000857Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability
Auteurs : François Bonneaux [France] ; Edith Dellacherie [France]Source :
- Journal of Protein Chemistry [ 0277-8033 ] ; 1995-01-01.
Descripteurs français
English descriptors
- KwdEn :
- Aldehyde, Aldehydic, Aldehydic dextrans, Aldehydic functions, Amadori, Amadori rearrangement, Amino groups, Bonneaux, Borohydride, Carboxamidobenzaldehyde, Carboxamidobenzaldehyde dextran, Conjugate, Covalent, Dellacherie, Dextran, Dextrans, Elution profiles, Fixation, Free hemoglobin, Glucose, Hemoglobin, Imine, Imine bonds, Imine linkages, Ketoamine, Labrude, Lysine, Mmol, Nabh4, Nabh4 treatment, Other hand, Oxidized, Oxidized conjugates, Oxidized dextran, Permeation chromatography, Phosphate buffer, Polymer, Rearrangement, Reductive treatment, Same conditions, Sodium borohydride, Sulfated, Ultrogel, Unreacted aldehydes, Unsulfated.
- Teeft :
- Aldehyde, Aldehydic, Aldehydic dextrans, Aldehydic functions, Amadori, Amadori rearrangement, Amino groups, Bonneaux, Borohydride, Carboxamidobenzaldehyde, Carboxamidobenzaldehyde dextran, Conjugate, Covalent, Dellacherie, Dextran, Dextrans, Elution profiles, Fixation, Free hemoglobin, Glucose, Hemoglobin, Imine, Imine bonds, Imine linkages, Ketoamine, Labrude, Lysine, Mmol, Nabh4, Nabh4 treatment, Other hand, Oxidized, Oxidized conjugates, Oxidized dextran, Permeation chromatography, Phosphate buffer, Polymer, Rearrangement, Reductive treatment, Same conditions, Sodium borohydride, Sulfated, Ultrogel, Unreacted aldehydes, Unsulfated.
Abstract
Abstract: Formation and stability of different aldehydic dextran-hemoglobin conjugates were studied. Two types of polymers were used: sulfated or unsulfated oxidized dextrans and 4-carboxamidobenzaldehyde dextran. Periodate-oxidized dextran forms imine and ketoamine linkages by reaction with hemoglobin and the obtained conjugates are not completely stable, as their molecular size increases with time or decreases after incubation with lysine. The sulfated conjugates are more sensitive to lysine action than the unsulfated ones, which is consistent with the decreased possibilities of Amadori rearrangement. Therefore, this proves the importance of ketoamines for ensuring the cohesion of oxidized dextran-based conjugates. Carboxamidobenzaldehyde dextran forms only imine linkages with hemoglobin and the corresponding conjugates possess a marked instability in the absence of reductive treatment. The different types of conjugates could be stabilized by a sodium borohydride treatment in a satisfying manner.
Url:
DOI: 10.1007/BF01902838
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability</title><author><name sortKey="Bonneaux, Francois" sort="Bonneaux, Francois" uniqKey="Bonneaux F" first="François" last="Bonneaux">François Bonneaux</name><affiliation wicri:level="1"><mods:affiliation>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex, France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex</wicri:regionArea></affiliation></author><author><name sortKey="Dellacherie, Edith" sort="Dellacherie, Edith" uniqKey="Dellacherie E" first="Edith" last="Dellacherie">Edith Dellacherie</name><affiliation wicri:level="1"><mods:affiliation>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex, France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:3FD0F4AF8405173352FDF91B8922CB84C1C8DEFC</idno><date when="1995" year="1995">1995</date><idno type="doi">10.1007/BF01902838</idno><idno type="url">https://api.istex.fr/document/3FD0F4AF8405173352FDF91B8922CB84C1C8DEFC/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000856</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000856</idno><idno type="wicri:Area/Istex/Curation">000856</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability</title><author><name sortKey="Bonneaux, Francois" sort="Bonneaux, Francois" uniqKey="Bonneaux F" first="François" last="Bonneaux">François Bonneaux</name><affiliation wicri:level="1"><mods:affiliation>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex, France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex</wicri:regionArea></affiliation></author><author><name sortKey="Dellacherie, Edith" sort="Dellacherie, Edith" uniqKey="Dellacherie E" first="Edith" last="Dellacherie">Edith Dellacherie</name><affiliation wicri:level="1"><mods:affiliation>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex, France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, BP 451, F-54001, Nancy Cedex</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Protein Chemistry</title><title level="j" type="abbrev">J Protein Chem</title><idno type="ISSN">0277-8033</idno><idno type="eISSN">1573-4943</idno><imprint><publisher>Kluwer Academic Publishers-Plenum Publishers</publisher><pubPlace>New York</pubPlace><date type="published" when="1995-01-01">1995-01-01</date><biblScope unit="volume">14</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="5">5</biblScope></imprint><idno type="ISSN">0277-8033</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0277-8033</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldehyde</term><term>Aldehydic</term><term>Aldehydic dextrans</term><term>Aldehydic functions</term><term>Amadori</term><term>Amadori rearrangement</term><term>Amino groups</term><term>Bonneaux</term><term>Borohydride</term><term>Carboxamidobenzaldehyde</term><term>Carboxamidobenzaldehyde dextran</term><term>Conjugate</term><term>Covalent</term><term>Dellacherie</term><term>Dextran</term><term>Dextrans</term><term>Elution profiles</term><term>Fixation</term><term>Free hemoglobin</term><term>Glucose</term><term>Hemoglobin</term><term>Imine</term><term>Imine bonds</term><term>Imine linkages</term><term>Ketoamine</term><term>Labrude</term><term>Lysine</term><term>Mmol</term><term>Nabh4</term><term>Nabh4 treatment</term><term>Other hand</term><term>Oxidized</term><term>Oxidized conjugates</term><term>Oxidized dextran</term><term>Permeation chromatography</term><term>Phosphate buffer</term><term>Polymer</term><term>Rearrangement</term><term>Reductive treatment</term><term>Same conditions</term><term>Sodium borohydride</term><term>Sulfated</term><term>Ultrogel</term><term>Unreacted aldehydes</term><term>Unsulfated</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Aldehyde</term><term>Aldehydic</term><term>Aldehydic dextrans</term><term>Aldehydic functions</term><term>Amadori</term><term>Amadori rearrangement</term><term>Amino groups</term><term>Bonneaux</term><term>Borohydride</term><term>Carboxamidobenzaldehyde</term><term>Carboxamidobenzaldehyde dextran</term><term>Conjugate</term><term>Covalent</term><term>Dellacherie</term><term>Dextran</term><term>Dextrans</term><term>Elution profiles</term><term>Fixation</term><term>Free hemoglobin</term><term>Glucose</term><term>Hemoglobin</term><term>Imine</term><term>Imine bonds</term><term>Imine linkages</term><term>Ketoamine</term><term>Labrude</term><term>Lysine</term><term>Mmol</term><term>Nabh4</term><term>Nabh4 treatment</term><term>Other hand</term><term>Oxidized</term><term>Oxidized conjugates</term><term>Oxidized dextran</term><term>Permeation chromatography</term><term>Phosphate buffer</term><term>Polymer</term><term>Rearrangement</term><term>Reductive treatment</term><term>Same conditions</term><term>Sodium borohydride</term><term>Sulfated</term><term>Ultrogel</term><term>Unreacted aldehydes</term><term>Unsulfated</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Glucose</term><term>Polymère</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Formation and stability of different aldehydic dextran-hemoglobin conjugates were studied. Two types of polymers were used: sulfated or unsulfated oxidized dextrans and 4-carboxamidobenzaldehyde dextran. Periodate-oxidized dextran forms imine and ketoamine linkages by reaction with hemoglobin and the obtained conjugates are not completely stable, as their molecular size increases with time or decreases after incubation with lysine. The sulfated conjugates are more sensitive to lysine action than the unsulfated ones, which is consistent with the decreased possibilities of Amadori rearrangement. Therefore, this proves the importance of ketoamines for ensuring the cohesion of oxidized dextran-based conjugates. Carboxamidobenzaldehyde dextran forms only imine linkages with hemoglobin and the corresponding conjugates possess a marked instability in the absence of reductive treatment. The different types of conjugates could be stabilized by a sodium borohydride treatment in a satisfying manner.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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