Optimization of magnetization transfer experiments to measure first- order rate constants and spin-lattice relaxation times

NMR in Biomedicine

Volumn 9, Issue 3, 1996, Pages 135-139

  Katki, Hormuzd ^a,b   Weiss, George H ^a   Kiefer, James E ^a   Taitelbaum, Haim ^c   Spencer, Richard G S ^d  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b CARNEGIE MELLON UNIVERSITY   (United States)

^c BAR ILAN UNIVERSITY   (Israel)

^d NATIONAL INSTITUTE ON AGING   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CREATINE KINASE; CREATINE PHOSPHATE;

ANIMAL; ARTICLE; KINETICS; MAGNETISM; MATHEMATICAL COMPUTING; METABOLISM; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RAT;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANIMALS; CREATINE KINASE; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MAGNETICS; MATHEMATICAL COMPUTING; PHOSPHOCREATINE; RATS;

ANIMALIA;

EID: 0030152409     PISSN: 09523480     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1492(199605)9:3<135::AID-NBM404>3.0.CO;2-H     Document Type: Article

References (14)

1. Rydzy, M., Deslaurier, R., Smith, I. C. P. and Saunders, J. K. Optimization of magnetization transfer measurements: statistical analysis by stochastic simulation. Application to creatine kinase kinetics, Magn. Reson. Med. 15, 260-274 (1990).
2. Forsén, S. and Huffman, R. A. Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance. J. Chem. Phys. 39, 2892-2901 (1963).
3. Forsén, S. and Hoffman, R. A. Exchange rates by nuclear magnetic multiple resonance. III. Exchange reactions in systems with several nonequivalent sites. J. Chem. Phys. 40, 1189-1196 (1964).
4. Hoffman, R. A. and Forsén, S. Transient and steady-state Overhauser experiments in the investigaton of relaxation processes. Analogies between chemical exchange and relaxation. J. Chem. Phys. 45, 1189-1196 (1966).
5. Alger, J. R. and Shulman, R. G. NMR studies of enzymatic rates in vitro and in vivo by magnetization transfer. Q. Rev. Biophs. 17, 83-124 (1984).
6. 31Phosphorus nuclear magnetic resonance magnetization transfer measurement of exchange reactions in vivo. In Biomedical Magnetic Resonance, ed. by T. L. James and A. R. Margulis, pp. 209-230. Radiology Research and Education Foundation, San Francisco, CA (1984).
7. Taitelbaum, H., Weiss, G. H. and Spencer, R. G. S. Optimization of magnetic transfer experiments for kinetic rate measurements. NMR Biomed. 7, 287-292 (1994).
8. Weiss, G. H., Gupta, R. K., Ferretti, J. A. and Becker, E. D. The choice of optimal parameters for measurement of spin-lattice relaxation times. I. Mathematical formulation. J. Magn. Reson. 37, 369-379 (1980).
9. Weiss, G. H. and Ferretti, J. A. Optimal design of relaxation time experiments. Prog. Magn. Reson. Spect. 20, 317-335 (1988).
10. 1. J. Magn. Reson. 105, 59-64 (1993).
11. 1. J. Magn. Reson. 109, 166-171 (1994).
12. 31P-nuclear magnetic resonance double saturation transfer experiments. Biophys. J. 54, 921-929 (1988).
13. 31P magnetization transfer studies of creatine kinase kinetics in living rabbit brain Magn. Reson. Med. 5, 1-12 (1987).
14. 13C NMR measurement of flux through alanine aminotransferase by inversion- and saturation-transfer methods. J. Magn. Reson. 64, 243-254 (1985).