Meeting Banner
Abstract #2427

Effect of Albumin on Longitudinal Relaxation of [1-13C1]-Pyruvate

Karlos X. Moreno1, Scott Sabelhaus1, Craig R. Malloy1, A Dean Sherry1, Matthew E. Merritt1

1Advanced Imaging Research Center, UT Southwestern Medical Center, Dallas, Tx, USA

Pyruvate binds to albumin. In the absence of albumin, the metabolic products of 2 mM hyperpolarized-[1-13C1]-pyruvate (HP-Pyr) are easily detected in the isolated heart but much higher [pyruvate] is required in the presence of albumin. The T1 of [1-13C1]-pyruvate is significantly reduced in the presence of albumin containing fatty acids and even more prominent in the presence of fatty acid-free albumin. Albumin catalyzes the relatively slow exchange of pyruvate methyl protons with solvent protons, suggesting transient covalent binding to albumin. The kinetics of these complex pyruvate/albumin interactions may play a significant role in hyperpolarized 13C imaging in vivo.