Abstract #0477

Heteronuclear cross- relaxation and polarization transfer effects enable spectroscopic measurements of enzymatic activity by hyperpolarized proton NMR.

Piotr Dzien*¹, Anne Fages*², Kevin Michael Brindle³, Markus Schwaiger¹, and Lucio Frydman²

¹Nuklearmedizinische Klinik und Poliklinik Klinikum rechts der Isar der TUM, Technische Universität München, Munich, Germany, ²Chemical Physics, Weizmann Institute of Science, Rehovot, Israel, ³CRUK Cambridge Institute, University of Cambridge, Cambridge, United Kingdom

Disolution DNP increases the sensitivity of 13C MR sufficiently to allow real time measurements of 13C- labelled substrates and products of their metabolism in vivo. While advantages could also result from hyperpolarized observations based on 1H MR, the fast relaxation times of 1H resonances prevent in vivo applications of this kind. Here we demonstrate, in vitro, that a substantial enhancement of the 1H resonance of [1-1H, 2,2,2-2H3,1-13C] acetaldehyde, produced in situ by solutions containing purified yeast Pyruvate Decarboxylase (yPDC) from 13C - hyperpolarized [U-2H3,2-13C] pyruvate, can be achieved. This enhancement can arise from either spontaneous or INEPT-driven 13C --> 1H polarization transfers.

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