Publication | Closed Access
The nature of the stable noncovalent dimers of band 3 protein from erythrocyte membranes in solutions of Triton X‐100
50
Citations
10
References
1983
Year
Membrane StructureProteinlipid InteractionMolecular BiologyProtein Phase SeparationAnalytical UltracentrifugationTriton X‐100Protein FoldingMembrane TransportBiophysicsProtein ChemistryBiochemistryMembrane BiologyMembrane SystemBiomolecular ScienceMembrane BiophysicsNatural SciencesStable DimersBand 3MedicineStable Noncovalent Dimers
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.
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