Studies on the topographical localization of the binding sites for substrate and for actin on the enzymes, glyceraldehydephosphate dehydrogenase and phosphofructokinase
- 1 January 1986
- journal article
- research article
- Published by Elsevier in International Journal of Biochemistry
- Vol. 18 (5) , 445-451
- https://doi.org/10.1016/0020-711x(86)90187-4
Abstract
No abstract availableThis publication has 33 references indexed in Scilit:
- Evidence for the spatial separation of the binding sites for substrate and for cytoskeletal proteins on the enzyme aldolaseInternational Journal of Biochemistry, 1986
- Role of lysine residues in the binding of glyceraldehyde-3-phosphate dehydrogenase to human erythrocyte membranesBiochemical and Biophysical Research Communications, 1983
- Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde 3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscleBiochemistry, 1983
- Retention of allosteric properties in an inactive, proteolyzed form of phosphofructokinaseBiochemistry, 1983
- Number and evolutionary conservation of α- and β-tubulin and cytoplasmic β- and γ-actin genes using specific cloned cDNA probesCell, 1980
- Structure and control of phosphofructokinase from Bacillus stearothermophilusNature, 1979
- Association of Glyceraldehyde‐3‐Phosphate Dehydrogenase with the Particulate Fraction of Chicken Skeletal MuscleEuropean Journal of Biochemistry, 1975
- Equilibrium binding study of the interaction of fructose 6-phosphate and fructose 1,6-bisphosphate with rabbit muscle phosphofructokinaseBiochemistry, 1975
- The effect of trypsin treatment on rabbit muscle phosphofructokinaseArchives of Biochemistry and Biophysics, 1974
- Resolution of Bacterial Proteins by Polyacrylamide Gel Electrophoresis on SlabsJournal of Biological Chemistry, 1974