True Arrhenius Relationships of Human Lactate Dehydrogenase

The pyruvate and NADH concentrations and the buffer pH which gave maximal activity with LDH isoenzymes derived from human heart and liver tissue were established for the temperatures 25°C, 30°C, 35°C, 37°C, 40°C, 45°C, and 50°C. The velocities of the LDH isoenzymes using these maximal assay conditions were used to obtain Arrhenius plots, i.e. log initial velocity against inverse ab-solute temperature. The Arrhenius plots were linear with both isoenzyme preparations up to 45°C. Between 45°C and 50°C it appe-ared that this linear relationship no longer held, particularly with the liver tissue. When the activation energies were calculated both isoenzyme preparations exhibited several points of inflexion, in each case occuring at the same temperatures. These inflexions repre-sent a change in the reaction kinetics, possibly a conformational change in the enzyme. The results also indicate that the LDH 1 and2 isoenzymes are more efficient than LDH 4 and 5