Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability
Identifieur interne : 002570 ( Main/Curation ); précédent : 002569; suivant : 002571Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability
Auteurs : François Bonneaux [France] ; Édith Dellacherie [France]Source :
- Journal of Protein Chemistry [ 0277-8033 ] ; 1995-01-01.
Descripteurs français
- KwdFr :
- Wicri :
- topic : Benzaldéhydes, Dextrane, Glucose, Hémoglobines, Oxydoréduction, Polymère.
English descriptors
- KwdEn :
- Aldehyde, Aldehydic, Aldehydic dextrans, Aldehydic functions, Amadori, Amadori rearrangement, Amino groups, Benzaldehydes (chemistry), Bonneaux, Borohydride, Carboxamidobenzaldehyde, Carboxamidobenzaldehyde dextran, Conjugate, Covalent, Dellacherie, Dextran, Dextrans, Dextrans (chemistry), Elution profiles, Fixation, Free hemoglobin, Glucose, Hemoglobin, Hemoglobins (chemistry), Imine, Imine bonds, Imine linkages, Ketoamine, Labrude, Lysine, Mmol, Nabh4, Nabh4 treatment, Other hand, Oxidation-Reduction, Oxidized, Oxidized conjugates, Oxidized dextran, Permeation chromatography, Phosphate buffer, Polymer, Rearrangement, Reductive treatment, Same conditions, Sodium borohydride, Sulfated, Ultrogel, Unreacted aldehydes, Unsulfated.
- MESH :
- chemical , chemistry : Benzaldehydes, Dextrans, Hemoglobins.
- 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, Oxidation-Reduction, 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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<term>Glucose</term>
<term>Hemoglobin</term>
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<term>Imine linkages</term>
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<term>Mmol</term>
<term>Nabh4</term>
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<term>Oxidized dextran</term>
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<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>
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<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>
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<wicri:regionArea>Laboratorie de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, Nancy</wicri:regionArea>
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<region type="old region">Lorraine (région)</region>
<settlement type="city">Nancy</settlement>
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<author><name sortKey="Dellacherie, E" sort="Dellacherie, E" uniqKey="Dellacherie E" first="E" last="Dellacherie">Édith Dellacherie</name>
<affiliation><country>France</country>
<placeName><settlement type="city">Nancy</settlement>
<region type="region" nuts="2">Grand Est</region>
<region type="region" nuts="2">Lorraine (région)</region>
</placeName>
<orgName type="laboratoire" n="5">Laboratoire réactions et génie des procédés</orgName>
<orgName type="university">Université de Lorraine</orgName>
<orgName type="institution">Centre national de la recherche scientifique</orgName>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1995">1995</date>
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<idno type="wicri:doubleKey">0277-8033:1995:Bonneaux F:fixation:of:various</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Fixation of various aldehydic dextrans onto human hemoglobin: study of conjugate stability.</title>
<author><name sortKey="Bonneaux, F" sort="Bonneaux, F" uniqKey="Bonneaux F" first="F" last="Bonneaux">F. Bonneaux</name>
<affiliation wicri:level="3"><nlm:affiliation>Laboratorie de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, Nancy, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Laboratorie de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, Nancy</wicri:regionArea>
<placeName><region type="region">Grand Est</region>
<region type="old region">Lorraine (région)</region>
<settlement type="city">Nancy</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Dellacherie, E" sort="Dellacherie, E" uniqKey="Dellacherie E" first="E" last="Dellacherie">Édith Dellacherie</name>
<affiliation><country>France</country>
<placeName><settlement type="city">Nancy</settlement>
<region type="region" nuts="2">Grand Est</region>
<region type="region" nuts="2">Lorraine (région)</region>
</placeName>
<orgName type="laboratoire" n="5">Laboratoire réactions et génie des procédés</orgName>
<orgName type="university">Université de Lorraine</orgName>
<orgName type="institution">Centre national de la recherche scientifique</orgName>
</affiliation>
</author>
</analytic>
<series><title level="j">Journal of protein chemistry</title>
<idno type="ISSN">0277-8033</idno>
<imprint><date when="1995" type="published">1995</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzaldehydes (chemistry)</term>
<term>Dextrans (chemistry)</term>
<term>Hemoglobins (chemistry)</term>
<term>Oxidation-Reduction</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Benzaldéhydes ()</term>
<term>Dextrane ()</term>
<term>Hémoglobines ()</term>
<term>Oxydoréduction</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Benzaldehydes</term>
<term>Dextrans</term>
<term>Hemoglobins</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Oxidation-Reduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Benzaldéhydes</term>
<term>Dextrane</term>
<term>Hémoglobines</term>
<term>Oxydoréduction</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">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>
</PubMed>
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