Abstract
Creatine kinase (CK) catalyzes the reversible phosphorylation of MgADP by phosphocreatine and thus regulates cellular concentrations of ADP and ATP. The temperature dependence of this reaction has been determined in rat brain in vivo between 30 and 40°C using31P NMR saturation transfer measurements. The pseudo-first-order rate constant for the forward CK reaction, kf, varies little with temperature over this range, with an apparent activation energy Ea= 14.2 ± 4.9 kJ/mol. This is considerably lower than the values of Eafor isolated CK enzymes. However, when changes in [MgADP] and [H+] with temperature are considered, a substrate concentration-independent value of Ea= 65.3 ± 9.7 kJ/mol is obtained for the maximum forward reaction velocity Vmax. This agrees well with literature values for the isolated brain-type isoform of CK.Key words: creatine kinase, activation energy, temperature, brain, rat.
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