{"title":"两种亚基间接触突变的新异常血红蛋白:Hb hotel dieu β99 (G1) Asp→Gly和Hb pittie salpetriere β34 (B16) Val→Phe的功能研究","authors":"Joëlle Thillet, Nicole Arous, Jean Rosa","doi":"10.1016/0005-2795(81)90018-0","DOIUrl":null,"url":null,"abstract":"<div><p>The functional properties of two new abnormal hemoglobins with high oxygen affinity were studied. Hb Hôtel Dieu β99 (G1) Asp → Gly is situated in the α<sub>1</sub>β<sub>2</sub> contact. Hb Pitié Salpétrière β34 (B16) Val → Phe is situated in the α<sub>1</sub>β<sub>1</sub> contact. Both hemoglobins exhibited similar functional properties with a 10-fold increased oxygen affinity, a decreased cooperativity, a decreased Bohr effect and a normal or slightly decreased 2,3-diphosphoglycerate effect. The structure-function relationship is discussed in the light of these results.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"670 2","pages":"Pages 260-264"},"PeriodicalIF":0.0000,"publicationDate":"1981-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90018-0","citationCount":"9","resultStr":"{\"title\":\"Functional studies of two new abnormal hemoglobins with their mutation located at intersubunit contacts: Hb hotel dieu β99 (G1) Asp → Gly and Hb pitie salpetriere β34 (B16) Val → Phe\",\"authors\":\"Joëlle Thillet, Nicole Arous, Jean Rosa\",\"doi\":\"10.1016/0005-2795(81)90018-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The functional properties of two new abnormal hemoglobins with high oxygen affinity were studied. Hb Hôtel Dieu β99 (G1) Asp → Gly is situated in the α<sub>1</sub>β<sub>2</sub> contact. Hb Pitié Salpétrière β34 (B16) Val → Phe is situated in the α<sub>1</sub>β<sub>1</sub> contact. Both hemoglobins exhibited similar functional properties with a 10-fold increased oxygen affinity, a decreased cooperativity, a decreased Bohr effect and a normal or slightly decreased 2,3-diphosphoglycerate effect. The structure-function relationship is discussed in the light of these results.</p></div>\",\"PeriodicalId\":100165,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"volume\":\"670 2\",\"pages\":\"Pages 260-264\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-09-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2795(81)90018-0\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005279581900180\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581900180","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Functional studies of two new abnormal hemoglobins with their mutation located at intersubunit contacts: Hb hotel dieu β99 (G1) Asp → Gly and Hb pitie salpetriere β34 (B16) Val → Phe
The functional properties of two new abnormal hemoglobins with high oxygen affinity were studied. Hb Hôtel Dieu β99 (G1) Asp → Gly is situated in the α1β2 contact. Hb Pitié Salpétrière β34 (B16) Val → Phe is situated in the α1β1 contact. Both hemoglobins exhibited similar functional properties with a 10-fold increased oxygen affinity, a decreased cooperativity, a decreased Bohr effect and a normal or slightly decreased 2,3-diphosphoglycerate effect. The structure-function relationship is discussed in the light of these results.
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