Enzyme Adaptation Along a Heterothermic Tissue: The Visceral Heat Exchangers of the Bluefin Tuna
We measured enzyme activities along a heterothermic tissue, the visceral retia mirabilia of the bluefin tuna, to test current theories of enzyme temperature adaptation. The heterothermic tissue model is ideal for the study of fundamental temperature adaptation because it eliminates confounding effects of whole animal acclimation. Enzymes were measured at six positions along the rete at four temperatures (15, 20, 25, and 30°C). Five enzymes (aspartate aminotransferase, citrate synthase, glucose-6- phosphate dehydrogenase, glutamate dehydrogenase, and pyruvate kinase) exhibited a significant positive compensatory effect, with activity at the cold end of the rete 1.2-3.1 times higher than at the warm end. Two enzymes (alanine aminotransferase and lactate dehydrogenase) exhibited no significant compensation. On the basis of activation energies of enzymes along the rete, differences in activity were due to differences in enzyme concentration and not isozymes or enzyme modification. Analysis of the compensatory responses of the enzymes in light of their thermal sensitivities leads us to conclude that the pentose phosphate shunt is especially enhanced at the cold end of the rete.
Fudge DS, Stevens ED, and Ballantyne JS (1997) Enzyme adaptation along a heterothermic tissue: the visceral heat exchangers of the bluefin tuna. American Journal of Physiology 272, R1834-1840.
American Physiological Society