Correlation between subunit interactions and enzymic activity of phosphorylase a. method for determining equilibrium constants from initial rate measurements
- 3 February 1970
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 9 (3), 660-671
- https://doi.org/10.1021/bi00805a028
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- The effect of glucose on the sedimentation and catalytic activity of glycogen phosphorylaseBiochemical and Biophysical Research Communications, 1965
- The effect of 5′adenylic acid upon the association between bromthymol blue and muscle phosphorylase bBiochemical and Biophysical Research Communications, 1964
- Calibration of light‐scattering instruments: A critical surveyJournal of Polymer Science, 1962
- Physical properties of flagellin from Proteus vulgaris, a study involving the application of the archibald sedimentation principleArchives of Biochemistry and Biophysics, 1960
- Molecular Interactions in β-Lactoglobulin. III. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.22Journal of the American Chemical Society, 1960
- Equilibria in the Fibrinogen-Fibrin Conversion. III. Heats of Polymerization and Clotting of Fibrin Monomer1Journal of the American Chemical Society, 1955
- Calibration of light scattering photometers with LudoxJournal of Polymer Science, 1954
- Some Geometrical Factors in Light-Scattering ApparatusJournal of the Optical Society of America, 1951
- Absolute Intensity of Light Scattering from Pure Liquids and SolutionsThe Journal of Chemical Physics, 1950