Aftab A. Ansari, Lalit M. Bahuguna, Mark. Jenison , Heinrich V. Malling
{"title":"小鼠血红蛋白的免疫学比较","authors":"Aftab A. Ansari, Lalit M. Bahuguna, Mark. Jenison , Heinrich V. Malling","doi":"10.1016/0161-5890(78)90008-1","DOIUrl":null,"url":null,"abstract":"<div><p>Immunological properties of several mice hemoglobins bearing α chains 1 or 4 and β chains s, d<sub>maj</sub> or p<sub>min</sub> were compared using radioimmunoassays that involved inhibition by these hemoglobins of a reaction between<sup>125</sup>I-labeled C57BL/6 hemoglobin (α chain 1, β chain s) and horse antibody against C57BL/6 hemoglobin. SJL hemoglobin (α chains 1 and 4. β chains) and C57BL/6 hemoglobin were found to have identical relative association constants,<em>K</em><sub>0(rel)</sub>. The d<sub>maj</sub> hemoglobins from DBA/2 and AU/Ss mice (α chain 1, β chain d<sub>maj</sub>) were 3.3 to 3.6 times less reactive while the p<sub>min</sub> hemoglobin from AU/Ss mice was found to be 17 times weaker than C57BL/6 hemoglobin. These immunological differences correlate with the amino acid sequence differences in the β chains.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 8","pages":"Pages 557-560"},"PeriodicalIF":0.0000,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90008-1","citationCount":"6","resultStr":"{\"title\":\"Immunological comparison of mouse hemoglobins\",\"authors\":\"Aftab A. Ansari, Lalit M. Bahuguna, Mark. Jenison , Heinrich V. Malling\",\"doi\":\"10.1016/0161-5890(78)90008-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Immunological properties of several mice hemoglobins bearing α chains 1 or 4 and β chains s, d<sub>maj</sub> or p<sub>min</sub> were compared using radioimmunoassays that involved inhibition by these hemoglobins of a reaction between<sup>125</sup>I-labeled C57BL/6 hemoglobin (α chain 1, β chain s) and horse antibody against C57BL/6 hemoglobin. SJL hemoglobin (α chains 1 and 4. β chains) and C57BL/6 hemoglobin were found to have identical relative association constants,<em>K</em><sub>0(rel)</sub>. The d<sub>maj</sub> hemoglobins from DBA/2 and AU/Ss mice (α chain 1, β chain d<sub>maj</sub>) were 3.3 to 3.6 times less reactive while the p<sub>min</sub> hemoglobin from AU/Ss mice was found to be 17 times weaker than C57BL/6 hemoglobin. These immunological differences correlate with the amino acid sequence differences in the β chains.</p></div>\",\"PeriodicalId\":13265,\"journal\":{\"name\":\"Immunochemistry\",\"volume\":\"15 8\",\"pages\":\"Pages 557-560\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1978-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0161-5890(78)90008-1\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Immunochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0161589078900081\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Immunochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0161589078900081","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Immunological properties of several mice hemoglobins bearing α chains 1 or 4 and β chains s, dmaj or pmin were compared using radioimmunoassays that involved inhibition by these hemoglobins of a reaction between125I-labeled C57BL/6 hemoglobin (α chain 1, β chain s) and horse antibody against C57BL/6 hemoglobin. SJL hemoglobin (α chains 1 and 4. β chains) and C57BL/6 hemoglobin were found to have identical relative association constants,K0(rel). The dmaj hemoglobins from DBA/2 and AU/Ss mice (α chain 1, β chain dmaj) were 3.3 to 3.6 times less reactive while the pmin hemoglobin from AU/Ss mice was found to be 17 times weaker than C57BL/6 hemoglobin. These immunological differences correlate with the amino acid sequence differences in the β chains.