H. Guderley et Ia. Johnston, PLASTICITY OF FISH MUSCLE MITOCHONDRIA WITH THERMAL-ACCLIMATION, Journal of Experimental Biology, 199(6), 1996, pp. 1311-1317
Short-horned sculpin Myoxocephalus scorpius were acclimated to 5 and 1
5 degrees C to evaluate the impact of thermal acclimation upon maximal
rates of substrate oxidation by mitochondria and upon the thermal sen
sitivity of their ADP affinity, Cold acclimation virtually doubled max
imal rates of pyruvate oxidation at all experimental temperatures (2.5
, 7.5, 12.5 and 20 degrees C). Rates of palmitoyl carnitine oxidation
were also enhanced by cold acclimation, but to a lesser degree. At the
ir respective acclimation temperatures, the mitochondria attained simi
lar rates of pyruvate oxidation. For warm-acclimated sculpin, the Q(10
) values for mitochondrial pyruvate and palmitoyl carnitine oxidation
were higher between 2.5 and 7.5 degrees C than between 7.5 and 12.5 de
grees C or between 12.5 and 20 degrees C. In contrast, for cold-acclim
ated fish, the Q(10) values did not differ over these thermal ranges.
The Arrhenius activation energy for pyruvate oxidation was reduced by
cold acclimation (from 70 to 55 kJ mol(-1)), whereas that for palmitoy
l carnitine oxidation was unchanged (approximately 75 kJ mol(-1)). Col
d acclimation did not alter the ADP affinity of mitochondria at low te
mperatures but markedly increased the apparent K-m for ADP (K-m,K-app)
at 12.5 and 20 degrees C. At the acclimation temperatures, mitochondr
ial ADP K-m,K-app values did not differ. The loss of ADP affinity at h
igher temperatures may represent a cost of the enhanced maximal oxidat
ive capacity achieved during cold acclimation.