Publication | Open Access
5′-Nucleotidases in rat heart. Evidence for the occurrence of two soluble enzymes with different substrate specificities
95
Citations
18
References
1988
Year
Cardiac MuscleCardiomyopathyImp-preferring EnzymeCellular EnzymologyBiochemistryAldo-keto ReductaseBioenergeticsEnzyme CatalysisPhysiologySoluble EnzymesStructure-function Enzyme KineticsRat HeartMetabolismMedicineSoluble ProteinsDifferent Substrate SpecificitiesProtein PhosphorylationOxidative Stress
Chromatography of soluble proteins from rat heart on phosphocellulose columns separates two 5'-nucleotidases. The first to emerge from the column shows a preference for AMP over IMP as substrate, whereas the second shows a preference for IMP over AMP. The properties of the IMP-preferring enzyme, including the conditions under which it is eluted from phosphocellulose columns, show it to be the enzyme studied by Itoh, Oka & Ozasa [Biochem. J. (1986) 235, 847-851]. The kinetic properties of the AMP-preferring enzyme indicate that it is likely to be the enzyme responsible for the production of adenosine under conditions of hypoxia and increased work load, and with metabolic stresses such as a high load of acetate.
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