期刊论文详细信息
| FEBS Letters | |
| Band 3‐hemoglobin associations The band 3 tetramer is the oxyhemoglobin binding site | |
| Schuck, Peter1  Schubert, Dieter1  | |
| [1] Institut für Biophysik der JWG-Universität, Theodor-Stern-Kai 7, D-6000 Frankfurt am Main 70, Germany | |
| 关键词: Band 3 protein; Hemoglobin; Protein—protein association; Analytical ultracentrifugation; Erythrocyte membrane; | |
| DOI : 10.1016/0014-5793(91)81156-3 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
The associations between the band 3 protein of the human erythrocyte membrane and oxyhemoglobin, in solutions of a nonionic detergent, were studied by sedimentation equilibrium experiments in the analytical ultracentrifuge. The following results were obtained: (i) hemoglobin is bound virtually exclusively to the band 3 tetramer, but not to the monomer or dimer; (ii) the band 3 tetramer can bind up to four hemoglobin tetramers; (iii) unlike the unstable dimers of unmodified band 3, stable dimers crosslinked via S S-bridges also represent hemoglobin binding sites.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020295595ZK.pdf | 380KB |
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