The properties of lactate dehydrogenase were examined in two snake species, Nerodia rhombifera and Elaphe obsoleta, and a turtle species, Pseudemys scripta. Our purpose was to compare the LDH activity of reptiles with limited anaerobic capabilities with that of the well established diver Pseudemys. The Michaelis-Menten kinetics of LDH and its susceptibility to inhibition by elevated pyruvate concentrations were investigated in the brain and heart of the three species. All tissue incubations and enzyme activity determinations were done at a pH of 7.0 in order to stimulate a diving blood pH in the three species. In both tissues the LDH activity of the snakes was higher than that of Pseudemys at pyruvate concentrations ranging between .03 mM and .50 mM. The Km values of the snakes were lower than those of Pseudemys, suggesting a greater enzyme-substrate affinity in the snake tissues. The Vmax values were higher in the snake tissues indicating a faster conversion of substrate to product. Heart LDH activity was reduced to an equal extent by high pyruvate concentrations in each of the three species. Elaphe brain LDH was most susceptible to pyruvate inhibition, but Nerodia and Pseudemys brain LDH were inhibited to an equal extent. The results indicate that the kinetic behavior of brain and heart LDH of the three species is similar at a pH of 7.4 and a pH of 7.0. The results also suggest that the LDH of Pseudemys is no better adapted to withstand anaerobic conditions than that of Nerodia or Elaphe at a pH of 7.0.

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