LrgpV1, Main, Curation, bibRecord, 002D68

Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity

Identifieur interne : 002D68 ( Main/Curation ); précédent : 002D67; suivant : 002D69

Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity

Auteurs : D. Sacco [France] ; D. Klett-Zygmunt [France] ; C. Vigneron [France] ; Édith Dellacherie [France]

Source :

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology [ 0167-4838 ] ; 1990.

RBID : ISTEX:F772595A4D0975A9BEB79D4CFC1D984BF38716B0

Descripteurs français

Pascal (Inist)
- Capacité fixation, Composé conjugué, Dextran, Homme, Hémoglobine, Hémoprotéine, Interaction moléculaire, Oxygène.
Wicri :
- topic : Glucose, Homme, Oxygène, Phosphate, Polymère.

English descriptors

Abstract

Abstract: The interactions between various dextran phosphates and Hb (hemoglobin) were studied by measuring the oxygen-binding parameters of the mixtures. The effector properties of polymers were found to depend on the concentration of monoalkylmonophosphate groups on the polymers and also on their molecular weights. The covalent fixation of dextran phosphates bearing aldehydic groups to exyHb and deoxyHb was carried out. The oxygen-binding properties of the conjugates thus obtained depended upon the initial form of the protein. Thus, only the conjugates synthesized from deoxyHb exhibited a low oxygen affinity, which means that, in this case, the linkages between the dextran phosphate and the protein allow a permanent interaction of the phosphate groups with amines of the 2,3-diphosphoglycerate binding site. The Hill coefficient values of these conjugates were smaller than that of free Hb, corresponding to a loss of the cooperativity of the protein upon fixation of polymers. However, as these new conjugates are capable of unloading more O2 than blood when subjected to oxygen pressures corresponding to physiological conditions, they can be regarded as potential erythrocyte substitutes.

Url:

https://api.istex.fr/document/F772595A4D0975A9BEB79D4CFC1D984BF38716B0/fulltext/pdf

DOI: 10.1016/0167-4838(90)90285-N

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Links to Exploration step

ISTEX:F772595A4D0975A9BEB79D4CFC1D984BF38716B0

Le document en format XML

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<front><div type="abstract" xml:lang="en">Abstract: The interactions between various dextran phosphates and Hb (hemoglobin) were studied by measuring the oxygen-binding parameters of the mixtures. The effector properties of polymers were found to depend on the concentration of monoalkylmonophosphate groups on the polymers and also on their molecular weights. The covalent fixation of dextran phosphates bearing aldehydic groups to exyHb and deoxyHb was carried out. The oxygen-binding properties of the conjugates thus obtained depended upon the initial form of the protein. Thus, only the conjugates synthesized from deoxyHb exhibited a low oxygen affinity, which means that, in this case, the linkages between the dextran phosphate and the protein allow a permanent interaction of the phosphate groups with amines of the 2,3-diphosphoglycerate binding site. The Hill coefficient values of these conjugates were smaller than that of free Hb, corresponding to a loss of the cooperativity of the protein upon fixation of polymers. However, as these new conjugates are capable of unloading more O2 than blood when subjected to oxygen pressures corresponding to physiological conditions, they can be regarded as potential erythrocyte substitutes.</div>
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<author><name sortKey="Dellacherie, E" sort="Dellacherie, E" uniqKey="Dellacherie E" first="E." last="Dellacherie">Édith Dellacherie</name>
<affiliation wicri:level="1"><country xml:lang="fr">France</country>
<wicri:regionArea>Laboratoire de Chimie-Physique Macromoléculaire, UA-494 CNRS, ENSIC</wicri:regionArea>
<wicri:noRegion>ENSIC</wicri:noRegion>
<wicri:noRegion>ENSIC</wicri:noRegion>
<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>
<monogr></monogr>
<series><title level="j">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title>
<title level="j" type="abbrev">BBAPRO</title>
<idno type="ISSN">0167-4838</idno>
<imprint><publisher>ELSEVIER</publisher>
<date type="published" when="1990">1990</date>
<biblScope unit="volume">1041</biblScope>
<biblScope unit="issue">3</biblScope>
<biblScope unit="page" from="279">279</biblScope>
<biblScope unit="page" to="284">284</biblScope>
</imprint>
<idno type="ISSN">0167-4838</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0167-4838</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldehyde groups</term>
<term>Aldehydic</term>
<term>Aldehydic dextran phosphate</term>
<term>Aldehydic dextran phosphates</term>
<term>Aldehydic groups</term>
<term>Allosteric site</term>
<term>Amine</term>
<term>Anticlotting properties</term>
<term>Benesch</term>
<term>Bistris buffer</term>
<term>Blood substitution</term>
<term>Conjugate</term>
<term>Covalent fixation</term>
<term>Crude dextran phosphates</term>
<term>Deoxy form</term>
<term>Deoxyhb</term>
<term>Dextran</term>
<term>Dextran phosphate</term>
<term>Dextran phosphates</term>
<term>Diphosphate groups</term>
<term>Effector</term>
<term>Effector properties</term>
<term>Fixation</term>
<term>Glucose</term>
<term>Glucose units</term>
<term>Imine functions</term>
<term>Limit value</term>
<term>Mmol</term>
<term>Mmol phosphate</term>
<term>Molar ratio</term>
<term>Molecular weight</term>
<term>Other hand</term>
<term>Oxygen affinity</term>
<term>Oxygen carrier</term>
<term>Oxygen carriers</term>
<term>Oxyhb</term>
<term>Phosphate</term>
<term>Phosphate content</term>
<term>Phosphate groups</term>
<term>Polyanionic polymers</term>
<term>Polymer</term>
<term>Room temperature</term>
<term>Same conditions</term>
<term>Torr</term>
<term>Tris buffer</term>
<term>Various dextran phosphates</term>
<term>Weight ratio</term>
</keywords>
<keywords scheme="Teeft" xml:lang="en"><term>Aldehyde groups</term>
<term>Aldehydic</term>
<term>Aldehydic dextran phosphate</term>
<term>Aldehydic dextran phosphates</term>
<term>Aldehydic groups</term>
<term>Allosteric site</term>
<term>Amine</term>
<term>Anticlotting properties</term>
<term>Benesch</term>
<term>Bistris buffer</term>
<term>Blood substitution</term>
<term>Conjugate</term>
<term>Covalent fixation</term>
<term>Crude dextran phosphates</term>
<term>Deoxy form</term>
<term>Deoxyhb</term>
<term>Dextran</term>
<term>Dextran phosphate</term>
<term>Dextran phosphates</term>
<term>Diphosphate groups</term>
<term>Effector</term>
<term>Effector properties</term>
<term>Fixation</term>
<term>Glucose</term>
<term>Glucose units</term>
<term>Imine functions</term>
<term>Limit value</term>
<term>Mmol</term>
<term>Mmol phosphate</term>
<term>Molar ratio</term>
<term>Molecular weight</term>
<term>Other hand</term>
<term>Oxygen affinity</term>
<term>Oxygen carrier</term>
<term>Oxygen carriers</term>
<term>Oxyhb</term>
<term>Phosphate</term>
<term>Phosphate content</term>
<term>Phosphate groups</term>
<term>Polyanionic polymers</term>
<term>Polymer</term>
<term>Room temperature</term>
<term>Same conditions</term>
<term>Torr</term>
<term>Tris buffer</term>
<term>Various dextran phosphates</term>
<term>Weight ratio</term>
</keywords>
<keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Glucose</term>
<term>Phosphate</term>
<term>Polymère</term>
</keywords>
</textClass>
<langUsage><language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Abstract: The interactions between various dextran phosphates and Hb (hemoglobin) were studied by measuring the oxygen-binding parameters of the mixtures. The effector properties of polymers were found to depend on the concentration of monoalkylmonophosphate groups on the polymers and also on their molecular weights. The covalent fixation of dextran phosphates bearing aldehydic groups to exyHb and deoxyHb was carried out. The oxygen-binding properties of the conjugates thus obtained depended upon the initial form of the protein. Thus, only the conjugates synthesized from deoxyHb exhibited a low oxygen affinity, which means that, in this case, the linkages between the dextran phosphate and the protein allow a permanent interaction of the phosphate groups with amines of the 2,3-diphosphoglycerate binding site. The Hill coefficient values of these conjugates were smaller than that of free Hb, corresponding to a loss of the cooperativity of the protein upon fixation of polymers. However, as these new conjugates are capable of unloading more O2 than blood when subjected to oxygen pressures corresponding to physiological conditions, they can be regarded as potential erythrocyte substitutes.</div>
</front>
</TEI>
</ISTEX>
</double>
</record>

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Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity

Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity

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