| Literature DB >> 1959675 |
Abstract
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.Entities:
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Year: 1991 PMID: 1959675 DOI: 10.1016/0014-5793(91)81156-3
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124