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Proton NMR measurements of hydrogen exchange at the C-3 position of 3-hydroxybutyrate in suspensions of rat liver mitochondria.

Abstract:
Rat liver mitochondria suspended in buffer made with 2H2O catalyse exchange C-3 proton of added D-3-hydroxybutyrate with solvent deuterons. The kinetics of this process can be followed using spin-echo proton NMR. The observed isotope exchange velocity is sensitive to the activity of D-3-hydroxybutyrate dehydrogenase, which is an integral protein of the inner mitochondrial membrane. A method is described which can be used to obtain the specific isotope exchange velocity of the enzyme in the intact mitochondrion.
Authors:
HH Paul, KM Brindle, ID Campbell, DJ Smith
Journal:
FEBS Lett
Citation info:
163(2):185-188
Publication date:
14th Nov 1983
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