Hemoglobin Athens‐Georgia [α2 β2 40(C6)Arg→Lys] in association with β0‐thalassemia in Tunisia
We describe an Hb Athens‐Georgia (Hb A‐Ga)/β0‐thalassemia compound heterozygosity, found in a Tunisian patient. Oxygen binding studies of red cell suspensions of this patient, containing approximately 95% Hb A‐Ga, revealed an almost normal oxygen affinity. Nevertheless, dilute solutions of Hb A‐Ga s...
Gespeichert in:
| Veröffentlicht in: | American journal of hematology 1989-10, Vol.32 (2), p.117-122 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 122 |
|---|---|
| container_issue | 2 |
| container_start_page | 117 |
| container_title | American journal of hematology |
| container_volume | 32 |
| creator | Mrad, A. Kister, J. Feo, C. Poyart, C. Kastally, R. Blibech, R. Galacteros, F. Wajcman, H. |
| description | We describe an Hb Athens‐Georgia (Hb A‐Ga)/β0‐thalassemia compound heterozygosity, found in a Tunisian patient. Oxygen binding studies of red cell suspensions of this patient, containing approximately 95% Hb A‐Ga, revealed an almost normal oxygen affinity. Nevertheless, dilute solutions of Hb A‐Ga showed an increased overall oxygen affinity and decreased heme‐heme interaction. This could be explained by a tetrameric hemoglobin with normal oxygen binding properties but with increased dissociation into monomers or dimers, as a consequence of a structural abnormality within the α1β2 interface. Such an interpretation would explain the increased oxygen affinity reported in previous studies performed on heterozygous Hb A/Hb A‐Ga patients. |
| doi_str_mv | 10.1002/ajh.2830320208 |
| format | Article |
| fullrecord | <record><control><sourceid>wiley_pasca</sourceid><recordid>TN_cdi_pascalfrancis_primary_7288124</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>AJH2830320208</sourcerecordid><originalsourceid>FETCH-LOGICAL-p798-33795c843c176905768d7f41af19963b00d1fcbdfa35a263bd51e57007571823</originalsourceid><addsrcrecordid>eNpFkLtOwzAYhS0EEqWwMmdggCHltx3fxqiCFlSJgW4IRW5iN67SpIqDqm5MzIg3gQfpQ_RJMALR6b-c75zhIHSOYYAByLVelAMiKVACBOQB6mFQPJackUPUA8px2EEdoxPvFwAYJxJ6yI7NsplXzczVUdqVpva71_eRadq509HT9pNE2y8SJXA55FdpO9-9fUw2_jkKtPa-yZ3uXFNHa9eVAYTg7UpdBcksgz9Q05faeadP0ZHVlTdnf7OPHm9vpsNxPHkY3Q3TSbwSSsaUCsVymdAcC66ACS4LYROsLVaK0xlAgW0-K6ymTJPwKBg2TAAIJrAktI8uflNX2ue6sq2uc-ezVeuWut1kgkiJSRIw9YutXWU2_zKG7KfHLPSY7XvM0vvx_qLfNodr-w</addsrcrecordid><sourcetype>Index Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Hemoglobin Athens‐Georgia [α2 β2 40(C6)Arg→Lys] in association with β0‐thalassemia in Tunisia</title><source>Wiley Online Library All Journals</source><creator>Mrad, A. ; Kister, J. ; Feo, C. ; Poyart, C. ; Kastally, R. ; Blibech, R. ; Galacteros, F. ; Wajcman, H.</creator><creatorcontrib>Mrad, A. ; Kister, J. ; Feo, C. ; Poyart, C. ; Kastally, R. ; Blibech, R. ; Galacteros, F. ; Wajcman, H.</creatorcontrib><description>We describe an Hb Athens‐Georgia (Hb A‐Ga)/β0‐thalassemia compound heterozygosity, found in a Tunisian patient. Oxygen binding studies of red cell suspensions of this patient, containing approximately 95% Hb A‐Ga, revealed an almost normal oxygen affinity. Nevertheless, dilute solutions of Hb A‐Ga showed an increased overall oxygen affinity and decreased heme‐heme interaction. This could be explained by a tetrameric hemoglobin with normal oxygen binding properties but with increased dissociation into monomers or dimers, as a consequence of a structural abnormality within the α1β2 interface. Such an interpretation would explain the increased oxygen affinity reported in previous studies performed on heterozygous Hb A/Hb A‐Ga patients.</description><identifier>ISSN: 0361-8609</identifier><identifier>EISSN: 1096-8652</identifier><identifier>DOI: 10.1002/ajh.2830320208</identifier><identifier>CODEN: AJHEDD</identifier><language>eng</language><publisher>New York: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Anemias. Hemoglobinopathies ; Biological and medical sciences ; Diseases of red blood cells ; ektacytometric studies ; Hb Waco ; Hematologic and hematopoietic diseases ; Medical sciences ; oxygen binding</subject><ispartof>American journal of hematology, 1989-10, Vol.32 (2), p.117-122</ispartof><rights>Copyright © 1989 Wiley‐Liss, Inc., A Wiley Company</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fajh.2830320208$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fajh.2830320208$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7288124$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Mrad, A.</creatorcontrib><creatorcontrib>Kister, J.</creatorcontrib><creatorcontrib>Feo, C.</creatorcontrib><creatorcontrib>Poyart, C.</creatorcontrib><creatorcontrib>Kastally, R.</creatorcontrib><creatorcontrib>Blibech, R.</creatorcontrib><creatorcontrib>Galacteros, F.</creatorcontrib><creatorcontrib>Wajcman, H.</creatorcontrib><title>Hemoglobin Athens‐Georgia [α2 β2 40(C6)Arg→Lys] in association with β0‐thalassemia in Tunisia</title><title>American journal of hematology</title><description>We describe an Hb Athens‐Georgia (Hb A‐Ga)/β0‐thalassemia compound heterozygosity, found in a Tunisian patient. Oxygen binding studies of red cell suspensions of this patient, containing approximately 95% Hb A‐Ga, revealed an almost normal oxygen affinity. Nevertheless, dilute solutions of Hb A‐Ga showed an increased overall oxygen affinity and decreased heme‐heme interaction. This could be explained by a tetrameric hemoglobin with normal oxygen binding properties but with increased dissociation into monomers or dimers, as a consequence of a structural abnormality within the α1β2 interface. Such an interpretation would explain the increased oxygen affinity reported in previous studies performed on heterozygous Hb A/Hb A‐Ga patients.</description><subject>Anemias. Hemoglobinopathies</subject><subject>Biological and medical sciences</subject><subject>Diseases of red blood cells</subject><subject>ektacytometric studies</subject><subject>Hb Waco</subject><subject>Hematologic and hematopoietic diseases</subject><subject>Medical sciences</subject><subject>oxygen binding</subject><issn>0361-8609</issn><issn>1096-8652</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNpFkLtOwzAYhS0EEqWwMmdggCHltx3fxqiCFlSJgW4IRW5iN67SpIqDqm5MzIg3gQfpQ_RJMALR6b-c75zhIHSOYYAByLVelAMiKVACBOQB6mFQPJackUPUA8px2EEdoxPvFwAYJxJ6yI7NsplXzczVUdqVpva71_eRadq509HT9pNE2y8SJXA55FdpO9-9fUw2_jkKtPa-yZ3uXFNHa9eVAYTg7UpdBcksgz9Q05faeadP0ZHVlTdnf7OPHm9vpsNxPHkY3Q3TSbwSSsaUCsVymdAcC66ACS4LYROsLVaK0xlAgW0-K6ymTJPwKBg2TAAIJrAktI8uflNX2ue6sq2uc-ezVeuWut1kgkiJSRIw9YutXWU2_zKG7KfHLPSY7XvM0vvx_qLfNodr-w</recordid><startdate>198910</startdate><enddate>198910</enddate><creator>Mrad, A.</creator><creator>Kister, J.</creator><creator>Feo, C.</creator><creator>Poyart, C.</creator><creator>Kastally, R.</creator><creator>Blibech, R.</creator><creator>Galacteros, F.</creator><creator>Wajcman, H.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>IQODW</scope></search><sort><creationdate>198910</creationdate><title>Hemoglobin Athens‐Georgia [α2 β2 40(C6)Arg→Lys] in association with β0‐thalassemia in Tunisia</title><author>Mrad, A. ; Kister, J. ; Feo, C. ; Poyart, C. ; Kastally, R. ; Blibech, R. ; Galacteros, F. ; Wajcman, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p798-33795c843c176905768d7f41af19963b00d1fcbdfa35a263bd51e57007571823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Anemias. Hemoglobinopathies</topic><topic>Biological and medical sciences</topic><topic>Diseases of red blood cells</topic><topic>ektacytometric studies</topic><topic>Hb Waco</topic><topic>Hematologic and hematopoietic diseases</topic><topic>Medical sciences</topic><topic>oxygen binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mrad, A.</creatorcontrib><creatorcontrib>Kister, J.</creatorcontrib><creatorcontrib>Feo, C.</creatorcontrib><creatorcontrib>Poyart, C.</creatorcontrib><creatorcontrib>Kastally, R.</creatorcontrib><creatorcontrib>Blibech, R.</creatorcontrib><creatorcontrib>Galacteros, F.</creatorcontrib><creatorcontrib>Wajcman, H.</creatorcontrib><collection>Pascal-Francis</collection><jtitle>American journal of hematology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mrad, A.</au><au>Kister, J.</au><au>Feo, C.</au><au>Poyart, C.</au><au>Kastally, R.</au><au>Blibech, R.</au><au>Galacteros, F.</au><au>Wajcman, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hemoglobin Athens‐Georgia [α2 β2 40(C6)Arg→Lys] in association with β0‐thalassemia in Tunisia</atitle><jtitle>American journal of hematology</jtitle><date>1989-10</date><risdate>1989</risdate><volume>32</volume><issue>2</issue><spage>117</spage><epage>122</epage><pages>117-122</pages><issn>0361-8609</issn><eissn>1096-8652</eissn><coden>AJHEDD</coden><abstract>We describe an Hb Athens‐Georgia (Hb A‐Ga)/β0‐thalassemia compound heterozygosity, found in a Tunisian patient. Oxygen binding studies of red cell suspensions of this patient, containing approximately 95% Hb A‐Ga, revealed an almost normal oxygen affinity. Nevertheless, dilute solutions of Hb A‐Ga showed an increased overall oxygen affinity and decreased heme‐heme interaction. This could be explained by a tetrameric hemoglobin with normal oxygen binding properties but with increased dissociation into monomers or dimers, as a consequence of a structural abnormality within the α1β2 interface. Such an interpretation would explain the increased oxygen affinity reported in previous studies performed on heterozygous Hb A/Hb A‐Ga patients.</abstract><cop>New York</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><doi>10.1002/ajh.2830320208</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0361-8609 |
| ispartof | American journal of hematology, 1989-10, Vol.32 (2), p.117-122 |
| issn | 0361-8609 1096-8652 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_7288124 |
| source | Wiley Online Library All Journals |
| subjects | Anemias. Hemoglobinopathies Biological and medical sciences Diseases of red blood cells ektacytometric studies Hb Waco Hematologic and hematopoietic diseases Medical sciences oxygen binding |
| title | Hemoglobin Athens‐Georgia [α2 β2 40(C6)Arg→Lys] in association with β0‐thalassemia in Tunisia |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-13T01%3A45%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-wiley_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Hemoglobin%20Athens%E2%80%90Georgia%20%5B%CE%B12%20%CE%B22%2040(C6)Arg%E2%86%92Lys%5D%20in%20association%20with%20%CE%B20%E2%80%90thalassemia%20in%20Tunisia&rft.jtitle=American%20journal%20of%20hematology&rft.au=Mrad,%20A.&rft.date=1989-10&rft.volume=32&rft.issue=2&rft.spage=117&rft.epage=122&rft.pages=117-122&rft.issn=0361-8609&rft.eissn=1096-8652&rft.coden=AJHEDD&rft_id=info:doi/10.1002/ajh.2830320208&rft_dat=%3Cwiley_pasca%3EAJH2830320208%3C/wiley_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |