LrgpV1, Main, Exploration, bibRecord, 002570

Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability

Identifieur interne : 002570 ( Main/Exploration ); précédent : 002569; suivant : 002571

Fixation 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.

RBID : ISTEX:3FD0F4AF8405173352FDF91B8922CB84C1C8DEFC

Descripteurs français

KwdFr :
- Benzaldéhydes (), Dextrane (), Hémoglobines (), Oxydoréduction.
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:

https://api.istex.fr/document/3FD0F4AF8405173352FDF91B8922CB84C1C8DEFC/fulltext/pdf

DOI: 10.1007/BF01902838

Affiliations:

Le document en format XML

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<term>Aldehydic functions</term>
<term>Amadori</term>
<term>Amadori rearrangement</term>
<term>Amino groups</term>
<term>Benzaldehydes (chemistry)</term>
<term>Bonneaux</term>
<term>Borohydride</term>
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<term>Conjugate</term>
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<term>Dellacherie</term>
<term>Dextran</term>
<term>Dextrans</term>
<term>Dextrans (chemistry)</term>
<term>Elution profiles</term>
<term>Fixation</term>
<term>Free hemoglobin</term>
<term>Glucose</term>
<term>Hemoglobin</term>
<term>Hemoglobins (chemistry)</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>Oxidation-Reduction</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>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Benzaldéhydes ()</term>
<term>Dextrane ()</term>
<term>Hémoglobines ()</term>
<term>Oxydoréduction</term>
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<term>Hemoglobins</term>
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<term>Aldehydic functions</term>
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<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>
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<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>Oxidation-Reduction</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>
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<term>Dextrane</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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Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability

Fixation of various aldehydic dextrans onto human hemoglobin: Study of conjugate stability

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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