Rotational diffusion of band 3 in erythrocyte membranes. 2. Binding of cytoplasmic enzymes
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00228a026
Reference39 articles.
1. Partial structural characterization of the cytoplasmic domain of the erythrocyte membrane protein, band 3.
2. Structural and motional changes in glyceraldehyde-3-phosphate dehydrogenase upon binding to the band-3 protein of the erythrocyte membrane examined with [15N,2H]maleimide spin label and electron paramagnetic resonance.
3. A 1H n.m.r. study of the kinetic properties expressed by glyceraldehyde phosphate dehydrogenase in the intact human erythrocyte
4. Quantitative analysis of the association of human hemoglobin with the cytoplasmic fragment of band 3 protein.
5. Affinity of hemoglobin for the cytoplasmic fragment of human erythrocyte membrane band 3
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