期刊论文详细信息
FEBS Letters | |
The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X‐100 | |
Dorst, H.-J.1  Boss, K.1  Pappert, G.1  Flossdorf, J.2  Schubert, D.1  | |
[1] Max-Planck-Institut für Biophysik, D-6000 Frankfurt-am-Main 71 FRG;Gesellschaft für Biotechnologische Forschung mbH, D-3300 Braunschweig, FRG | |
关键词: Erythrocyte membrane; Band 3 protein; Stable noncovalent dimer; Association equilibrium; Triton X-100; Peroxide; | |
DOI : 10.1016/0014-5793(83)81168-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Stable noncovalent dimers of band 3 protein from human erythrocyte membranes, in which state the protein is thought to exist after solubilization by the nonionic detergent Triton X-100, do not occur when purified batches of the detergent are used. Instead, the protein is in a monomer/dimer/tetramer association equilibrium. The stable dimers do appear, however, when the detergent has been ‘aged’. They thus seem to be artifacts.
【 授权许可】
Unknown
【 预 览 】
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