Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity.
Identifieur interne : 002D34 ( Main/Exploration ); précédent : 002D33; suivant : 002D35Covalent fixation of hemoglobin to dextran phosphates decreases its oxygen affinity.
Auteurs : D. Sacco [France] ; D. Klett-Zygmunt ; C. Vigneron ; Édith Dellacherie [France]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 1990.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Hémoglobines, Oxygène, Oxyhémoglobines.
- Dextrane, Hémoglobines, Oxygène, Oxyhémoglobines, Phosphorylation.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Dextrans, Hemoglobins, Oxygen, Oxyhemoglobins.
- chemical , metabolism : Hemoglobins, Oxygen, Oxyhemoglobins.
- Phosphorylation.
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 oxyHb 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.
PubMed: 1702682
Affiliations:
- France
- Grand Est, Lorraine (région)
- Nancy
- Centre national de la recherche scientifique, Laboratoire réactions et génie des procédés, Université de Lorraine
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Le document en format XML
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Sacco</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire de Chimie-Physique Macromoléculaire, UA-494 CNRS, ENSIC, Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Chimie-Physique Macromoléculaire, UA-494 CNRS, 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="Klett Zygmunt, D" sort="Klett Zygmunt, D" uniqKey="Klett Zygmunt D" first="D" last="Klett-Zygmunt">D. Klett-Zygmunt</name></author><author><name sortKey="Vigneron, C" sort="Vigneron, C" uniqKey="Vigneron C" first="C" last="Vigneron">C. Vigneron</name></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">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="1990" type="published">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Dextrans (chemistry)</term><term>Hemoglobins (chemistry)</term><term>Hemoglobins (metabolism)</term><term>Oxygen (chemistry)</term><term>Oxygen (metabolism)</term><term>Oxyhemoglobins (chemistry)</term><term>Oxyhemoglobins (metabolism)</term><term>Phosphorylation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Dextrane ()</term><term>Hémoglobines ()</term><term>Hémoglobines (métabolisme)</term><term>Oxygène ()</term><term>Oxygène (métabolisme)</term><term>Oxyhémoglobines ()</term><term>Oxyhémoglobines (métabolisme)</term><term>Phosphorylation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dextrans</term><term>Hemoglobins</term><term>Oxygen</term><term>Oxyhemoglobins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemoglobins</term><term>Oxygen</term><term>Oxyhemoglobins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Hémoglobines</term><term>Oxygène</term><term>Oxyhémoglobines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Phosphorylation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dextrane</term><term>Hémoglobines</term><term>Oxygène</term><term>Oxyhémoglobines</term><term>Phosphorylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 oxyHb 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><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Nancy</li></settlement><orgName><li>Centre national de la recherche scientifique</li><li>Laboratoire réactions et génie des procédés</li><li>Université de Lorraine</li></orgName></list><tree><noCountry><name sortKey="Klett Zygmunt, D" sort="Klett Zygmunt, D" uniqKey="Klett Zygmunt D" first="D" last="Klett-Zygmunt">D. Klett-Zygmunt</name><name sortKey="Vigneron, C" sort="Vigneron, C" uniqKey="Vigneron C" first="C" last="Vigneron">C. Vigneron</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Sacco, D" sort="Sacco, D" uniqKey="Sacco D" first="D" last="Sacco">D. Sacco</name></region><name sortKey="Dellacherie, E" sort="Dellacherie, E" uniqKey="Dellacherie E" first="E" last="Dellacherie">Édith Dellacherie</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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