Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume 829, Issue 2, 10 June 1985, Pages 188-201
Regular papersMeasurements of exchange in the reaction catalysed by creatine kinase using 14C and 15N isotope labels and the NMR technique of saturation transfer
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Cited by (29)
<sup>31</sup>P saturation transfer spectroscopy predicts differential intracellular macromolecular association of ATP and ADP in skeletal muscle
2010, Journal of Biological ChemistryCitation Excerpt :Careful examination of Fig. 5A shows that this is not to be expected. At in vitro-like conditions (τc ∼0.3 ns), the T1 relaxation through the chemical shift anisotropy is very effective, and still, the MT effect of β-phosphoryl exchange is observed (24, 34). For higher values of the rotational correlation times, corresponding with ATP binding to medium-sized proteins, T1 becomes even longer.
The in vitro kinetics of mitochondrial and cytosolic creatine kinase determined by saturation transfer <sup>31</sup>P-NMR
1996, Biochimica et Biophysica Acta - BioenergeticsIn vitro determination of creatine kinase substrate fluxes using <sup>31</sup>P-nuclear magnetic resonance
1995, BBA - General SubjectsFast Inversion-Recovery Measurements in the Presence of a Saturating Field for a Two-Spin System in Chemical Exchange
1994, Journal of Magnetic Resonance, Series A
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