A comparative study of the binding of aldolase and glyceraldehyde-3-phosphate dehydrogenase to the human erythrocyte membrane
- 1 May 1982
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 215 (2) , 610-620
- https://doi.org/10.1016/0003-9861(82)90122-9
Abstract
No abstract availableThis publication has 39 references indexed in Scilit:
- Connections between cytoplasmic proteins and the erythrocyte membraneTrends in Biochemical Sciences, 1981
- Light-scattering measurements of hemoglobin binding to the erythrocyte membrane. Evidence for transmembrane effects related to a disulfonic stilbene binding to band 3Biochemistry, 1980
- Localization and membrane association of aldolase in human erythrocytesArchives of Biochemistry and Biophysics, 1980
- Structure of the anion-transport protein of the human erythrocyte membrane. Further studies on the fragments produced by proteolytic digestionBiochemical Journal, 1979
- Functional properties of human hemoglobin bound to the erythrocyte membraneBiochemistry, 1979
- The band 3 protein of the human red cell membrane: A reviewJournal of Supramolecular Structure, 1978
- Interaction of the aldolase and the membrane of human erythrocytesBiochemistry, 1977
- Binding of rabbit muscle aldolase to band 3, the predominant polypeptide of the human erythrocyte membraneBiochemistry, 1976
- Proteolytic dissection of band 3, the predominant transmembrane polypeptide of the human erythrocyte membraneBiochemistry, 1976
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971