Spectral and oxygen-release kinetic properties of human hemoglobin bound to the cytoplasmic fragment of band 3 protein in solution
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference14 articles.
1. Functional properties of human hemoglobin bound to the erythrocyte membrane
2. Light-scattering measurements of hemoglobin binding to the erythrocyte membrane. Evidence for transmembrane effects related to a disulfonic stilbene binding to band 3
3. Quantitative analysis of the association of human hemoglobin with the cytoplasmic fragment of band 3 protein.
4. Partial structural characterization of the cytoplasmic domain of the erythrocyte membrane protein, band 3.
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1. Hemoglobin Conjugated with a Band 3 N-terminus Derived Peptide as an Oxygen Carrier;Artificial Cells, Blood Substitutes, and Biotechnology;2009-01
2. Kinetics of Reaction of Nitrite with Deoxy Hemoglobin after Rapid Deoxygenation or Predeoxygenation by Dithionite Measured in Solution and Bound to the Cytoplasmic Domain of Band 3 (SLC4A1);Biochemistry;2008-05-09
3. Fluorescence analysis of aldolase dissociation from the N-terminal of the cytoplasmic domain of band 3 induced by lanthanide;Biochemical and Biophysical Research Communications;2003-04
4. Heme Redox Properties of S-Nitrosated Hemoglobin A0 and Hemoglobin S;Journal of Biological Chemistry;2002-04
5. Characterization of the pH dependence of hemoglobin binding to band 3;Biochimica et Biophysica Acta (BBA) - Biomembranes;1998-04
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