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

L. J. Friesen-Waldner; C. N. Wiens; T. P. Wade; K. Thind; K. P. Sinclair; Y. Hovav; J. M. Gomori; J. Sosna; C. A. McKenzie; R. Katz-Brull

doi:10.1039/C4CC05418K

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

L. J. Friesen-Waldner,^a C. N. Wiens,^a T. P. Wade,^a K. Thind,^a K. P. Sinclair,^a Y. Hovav,^b J. M. Gomori,^c J. Sosna,^c C. A. McKenzie ‡^a and R. Katz-Brull ‡*^c

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^a Department of Medical Biophysics, Western University, London, Ontario, Canada

^b Weizmann Institute of Science, Rehovot, Israel

^c Department of Radiology, Hadassah-Hebrew University Medical Center, Jerusalem, Israel
E-mail: rkb@hadassah.org.il

Abstract

A specialized kinetic analysis of real-time hyperpolarized [1,1,2,2-D₄, 1-¹³C]choline ¹³C-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.

Chemical Communications

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

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

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