{"title":"spectrin α- 1片段与完整spectrin低聚物关联的定量评价","authors":"Nerida Cole, Gregory B. Ralston","doi":"10.1016/0020-711X(94)90067-1","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The α-I fragment of human spectrin that carries the binding site on the α-chain of spectrin for the β -chain has been purified from limited trypsin digests of spectrin by means of FPLC.</p></span></li><li><span>2.</span><span><p>2. The self-association of spectrin and the binding of the α-I fragment to spectrin heterodimers and to tetramers have been quantified through the use of gel electrophoresis, staining with Coomassie Blue, and quantification of the bound dye following elution with pyridine.</p></span></li><li><span>3.</span><span><p>3. The parameters of self-association were found to be consistent with those estimated from sedimentation equilibrium analysis.</p></span></li><li><span>4.</span><span><p>4. The data were consistent with a model in which both self-association and the binding of the α-I fragment are considered to occur through an intermediate in which the α-β interface is initially dissociated. The α-β interface in the heterodimer was found to be less stable than that of higher oligomers by approx. 3 kJ/mol.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 8","pages":"Pages 971-976"},"PeriodicalIF":0.0000,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90067-1","citationCount":"3","resultStr":"{\"title\":\"Quantitative assessment of the association of the α-I fragment of spectrin with oligomers of intact spectrin\",\"authors\":\"Nerida Cole, Gregory B. Ralston\",\"doi\":\"10.1016/0020-711X(94)90067-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. The α-I fragment of human spectrin that carries the binding site on the α-chain of spectrin for the β -chain has been purified from limited trypsin digests of spectrin by means of FPLC.</p></span></li><li><span>2.</span><span><p>2. The self-association of spectrin and the binding of the α-I fragment to spectrin heterodimers and to tetramers have been quantified through the use of gel electrophoresis, staining with Coomassie Blue, and quantification of the bound dye following elution with pyridine.</p></span></li><li><span>3.</span><span><p>3. The parameters of self-association were found to be consistent with those estimated from sedimentation equilibrium analysis.</p></span></li><li><span>4.</span><span><p>4. The data were consistent with a model in which both self-association and the binding of the α-I fragment are considered to occur through an intermediate in which the α-β interface is initially dissociated. The α-β interface in the heterodimer was found to be less stable than that of higher oligomers by approx. 3 kJ/mol.</p></span></li></ul></div>\",\"PeriodicalId\":13733,\"journal\":{\"name\":\"International Journal of Biochemistry\",\"volume\":\"26 8\",\"pages\":\"Pages 971-976\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711X(94)90067-1\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020711X94900671\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94900671","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Quantitative assessment of the association of the α-I fragment of spectrin with oligomers of intact spectrin
1.
1. The α-I fragment of human spectrin that carries the binding site on the α-chain of spectrin for the β -chain has been purified from limited trypsin digests of spectrin by means of FPLC.
2.
2. The self-association of spectrin and the binding of the α-I fragment to spectrin heterodimers and to tetramers have been quantified through the use of gel electrophoresis, staining with Coomassie Blue, and quantification of the bound dye following elution with pyridine.
3.
3. The parameters of self-association were found to be consistent with those estimated from sedimentation equilibrium analysis.
4.
4. The data were consistent with a model in which both self-association and the binding of the α-I fragment are considered to occur through an intermediate in which the α-β interface is initially dissociated. The α-β interface in the heterodimer was found to be less stable than that of higher oligomers by approx. 3 kJ/mol.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
