The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli
Open Access
- 1 July 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (13) , 4624-4630
- https://doi.org/10.1016/s0021-9258(17)30434-9
Abstract
No abstract availableThis publication has 36 references indexed in Scilit:
- pH dependence of the shape of the hemoglobin-oxygen equilibrium curveBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- A mathematical model for structure-function relations in hemoglobinJournal of Molecular Biology, 1972
- Stereochemistry of Cooperative Effects in HemoglobinCold Spring Harbor Symposia on Quantitative Biology, 1972
- The 5.5 A Resolution Structure of the Regulatory Enzyme, Aspartate TranscarbamylasePublished by Cold Spring Harbor Laboratory ,1972
- Spin-labeling studies of aspartate transcarbamylase. I. Effects of nucleotide binding and subunit separationBiochemistry, 1970
- Crystallographic Determination of Symmetry of Aspartate TranscarbamylaseNature, 1968
- New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide ChainNature, 1968
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- Effet des analogues de la L-thréonine et de la L-isoleucine sur la L-thréonine désaminaseJournal of Molecular Biology, 1962
- 366. Kinetic and tracer studies of the reactions of carbamoyl phosphate in aqueous solutionJournal of the Chemical Society, 1962