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   

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