Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase.
Open Access
- 1 February 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (3) , 1438-1442
- https://doi.org/10.1016/s0021-9258(19)68212-8
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanismPublished by Elsevier ,2004
- 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
- Isolation and characterization of glyceraldehyde-3-phosphate dehydrogenase from human erythrocyte membranesArchives of Biochemistry and Biophysics, 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
- Partial reversible inactivation of enzymes due to binding to the human erythrocyte membraneMolecular and Cellular Biochemistry, 1976
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971