[34] Covalently bound glutamate dehydrogenase for studies of subunit association and allosteric regulation
- 1 January 1976
- book chapter
- Published by Elsevier
- Vol. 44, 504-515
- https://doi.org/10.1016/s0076-6879(76)44036-3
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Reversible allosteric modulation of activity of immobilized hepatic glutamate dehydrogenaseBiochemical and Biophysical Research Communications, 1974
- Metabolic Compartmentation: Symbiotic, Organellar, Multienzymic, and MicroenvironmentalAnnual Review of Microbiology, 1974
- Kinetic behavior of enzymes in artificial membranes. Inhibition and reversibility effectsBiochemistry, 1974
- Effect of internal diffusion in heterogeneous enzyme systems: Evaluation of true kinetic parameters and substrate diffusivityJournal of Theoretical Biology, 1973
- In vitro assembly of aldolase. Kinetics of refolding, subunit reassociation, and reactivationBiochemistry, 1972
- Ligand binding and internal equilibiums in proteinsBiochemistry, 1972
- Ligand-induced dimer-to-tetramer transformation in cytosine triphosphate synthetaseBiochemistry, 1972
- Some modifications of the kinetic properties of bovine liver glutamate dehydrogenase (NAD(P)) covalently bound to a solid matrix of collagenFEBS Letters, 1971
- Hybridization of native and chemically modified enzymes. I. Development of a general method and its application to the study of the subunit structure of aldolaseBiochemistry, 1970
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965