31P nuclear magnetic resonance of bound substrates of arginine kinase reaction: chemical shifts in binary, ternary, quaternary, and transition state analog complexes.
Open Access
- 1 May 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (10), 3344-3350
- https://doi.org/10.1016/s0021-9258(17)40395-4
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- 31P NMR studies of the arginine kinase reaction. Equilibrium constants and exchange rates at stoichiometric enzyme concentration.Journal of Biological Chemistry, 1976
- Magnetic resonance study of the three-dimensional structure of creatine kinase-substrate complexes. Implications for substrate specificity and catalytic mechanism.Journal of Biological Chemistry, 1976
- 31P NMR of alkaline phosphataseBiochemical and Biophysical Research Communications, 1975
- 31P magnetic resonance of tRNA.Proceedings of the National Academy of Sciences, 1975
- Effects of anions on a monomeric and a dimeric arginine kinaseBiochemical Journal, 1975
- 31P chemical shifts in phosphate diester monoanions. Bond angle and torsional angle effectsBiochemical and Biophysical Research Communications, 1975
- Interaction of Mg2+ions with nucleoside triphosphates by phosphorus magnetic resonance spectroscopyNucleic Acids Research, 1975
- Determination of Intracellular pH by 31P Magnetic ResonanceJournal of Biological Chemistry, 1973
- Purification of Arginine Kinase from Lobster and a Study of Some Factors Affecting Its Reactivation*Biochemistry, 1967
- Nuclear Magnetic Resonance Spectra of Adenosine Di- and TriphosphateJournal of Biological Chemistry, 1962