Direct enzyme–substrate affinity determination by real-time hyperpolarized 13 C-MRS

Direct enzyme–substrate affinity determination by real-time hyperpolarized 13 C-MRS

A specialized kinetic analysis of real-time hyperpolarized [1,1,2,2-D 4 , 1- 13 C]choline 13 C-magnetic resonance spectroscopy enabled the determination of initial rates of metabolic enzyme activity (choline oxidase), enzyme–substrate affinity ( K m ), and inhibition. In a clinical MRI scanner, meta...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2014, Vol.50 (89), p.13801-13804
Hauptverfasser: Friesen-Waldner, L. J., Wiens, C. N., Wade, T. P., Thind, K., Sinclair, K. P., Hovav, Y., Gomori, J. M., Sosna, J., McKenzie, C. A., Katz-Brull, R.
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Sprache:eng
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Zusammenfassung:A specialized kinetic analysis of real-time hyperpolarized [1,1,2,2-D 4 , 1- 13 C]choline 13 C-magnetic resonance spectroscopy enabled the determination of initial rates of metabolic enzyme activity (choline oxidase), enzyme–substrate affinity ( K m ), and inhibition. In a clinical MRI scanner, metabolite levels lower than 16 μM were detected at a temporal resolution of 1 s.
ISSN:1359-7345
1364-548X
DOI:10.1039/C4CC05418K