STUDIES ON THE FORMATION OF AN ENZYME-SUBSTRATE COMPLEX BETWEEN MYOSIN AND ADENOSINETRIPHOSPHATE
- 1 August 1960
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 46 (8) , 1155-1166
- https://doi.org/10.1073/pnas.46.8.1155
Abstract
A methodology has been developed by which the concentration of ATP in a reaction system is continuously measured by recording the light emitted by the firefly luciferase-luciferin system. When in such a system, also containing phosphocreatine and creatine kinase, myosin is introduced, the decrease in luminescence is due to the binding of ATP by myosin, since the system could be so designed that all other factors were negligible. The enzyme-substrate binding takes place in a one to one molar ratio.This publication has 22 references indexed in Scilit:
- The preparation and properties of crystalline firefly luciferinArchives of Biochemistry and Biophysics, 1957
- THE EFFECT UPON ACTOMYOSIN OF STOICHIOMETRIC AMOUNTS OF ADENOSINETRIPHOSPHATE REGENERATED IN A COUPLED ENZYME SYSTEMThe Journal of general physiology, 1956
- THE EFFECT OF ADENOSINETRIPHOSPHATE UPON ACTOMYOSIN SOLUTIONS, STUDIED WITH A RECORDING DUAL BEAM LIGHT-SCATTERING PHOTOMETERThe Journal of general physiology, 1956
- Elementary Processes in Muscle Action: An Examination of Current ConceptsPhysiological Reviews, 1955
- ADENOSINETRIPHOSPHATE-CREATINE TRANSPHOSPHORYLASE .1. ISOLATION OF THE CRYSTALLINE ENZYME FROM RABBIT MUSCLE1954
- ADENOSINETRIOPHOSPHATE-CREATINE TRANSPHOSPHORYLASE .4. EQUILIBRIUM STUDIES1954
- The interaction of purified enolase with its activating metal ionsArchives of Biochemistry and Biophysics, 1953
- Postirradiation release of adenosine triphosphate from Escherichia coliBrArchives of Biochemistry and Biophysics, 1953
- Firefly luminescence in the study of energy transfer mechanisms. I. Substrate and enzyme determinationArchives of Biochemistry and Biophysics, 1952
- THE MOLECULAR TRANSFORMATIONS OF ACTIN .1. GLOBULAR ACTIN1952