AJP - Regulatory, Integrative and Comparative Physiology, Vol 234, Issue 3 136-R140, Copyright © 1978 by American Physiological Society
Controlling the highest lactate dehydrogenase activity known in nature
M. Guppy and P. W. Hochachka
In the shipjack, Euthynnus pelamis, white muscle appears to possess a
powerful anaerobic capacity as well as a significant carbohydrate based
aerobic potential. Lactate dehydrogenase occurs at higher activities than
found thus far anywhere else in nature and clearly functions in anaerobic
glycolysis. Alpha-glycerophosphate dehydrogenase also occurs in unusually
high activities and appears to play a role in aerobic glycolysis.
Regulation of these two reactions is accomplished by temperature, pH, and
creatine phosphate levels. High temperature, low pH, and low creatine
phosphate levels all appear to favor lactate dehydrogenase over
alpha-glycerophosphate dehydrogenase; low temperature, high pH, and high
creatine-phosphate levels, all expected during the quiescent state in this
species, and when metabolism in aerobic, all favor alpha-glycerophosphate
dehydrogenase activity.
