First published online August 25, 2003
Time course of the response of mitochondria from oxidative muscle during thermal acclimation of rainbow trout, Oncorhynchus mykiss
Patrice Bouchard and
Helga Guderley*
Département de Biologie, Université Laval,
Québec, Canada, G1K 7P4

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Fig. 1. Time course of changes in maximal rates of pyruvate oxidation by
mitochondria from oxidative muscle during warm and cold acclimation. Rates are
expressed per mg mitochondrial protein, per nmol ADP-ATP translocase (ANT),
per nmol cytochrome b (cyt. b) and per mg phospholipids.
Data are means ± S.E.M. When rates at a given assay
temperature during each acclimation experiment differ, they are followed by
different letters (P 0.05; ANOVA and Tukey's a posteriori
test). *Denotes a significant difference between final cold rate (week 10) and
initial cold rate (initial in warm acclimation). No differences were found
between final warm rate (week 8) and initial warm rate (initial in cold
acclimation). The number of individuals for each experiment is shown in
Table 1. NA, not available.
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Fig. 2. Time course of changes in maximal rates of palmitoyl carnitine oxidation by
mitochondria from oxidative muscle during warm and cold acclimation. Rates are
expressed per mg mitochondrial protein, per nmol ADP-ATP translocase (ANT),
per nmol cytochrome b (cyt. b) and per mg phospholipids.
Data are means ± S.E.M. When rates at a given assay
temperature during each acclimation experiment differ, they are followed by
different letters (P 0.05; ANOVA and Tukey's a posteriori
test). *Denotes a significant difference between final cold rate (week 10) and
initial cold rate (initial in warm acclimation). No differences were found
between final warm rate (week 8) and initial warm rate (initial in cold
acclimation). The number of individuals for each experiment is shown in
Table 1.
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Fig. 3. Ratio of mitochondrial rates of pyruvate oxidation to maximal activities of
cytochrome c oxidase (CCO) and citrate synthase (CS) during warm and
cold acclimation. Values are expressed per mU CCO and per mU CS. Data are
means ± S.E.M. When values at a given assay temperature
during each acclimation experiment differ, they are followed by different
letters (P 0.05; ANOVA and Tukey's a posteriori test).
The number of individuals in each experiment is shown in
Table 1.
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Fig. 4. Time course of changes in state 4 and oligomycin-inhibited state 4 (state
4ol) rates of pyruvate and palmitoyl carnitine oxidation by
mitochondria from oxidative muscle during warm and cold acclimation. Rates are
expressed per mg mitochondrial protein. Data are means ±
S.E.M. When rates at a given assay temperature during each
acclimation experiment differ, they are followed by different letters
(P 0.05; ANOVA and Tukey's a posteriori test).
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Fig. 5. Muscle aerobic capacity and mitochondrial protein content during thermal
acclimation. Data are means ± S.E.M. When values at a given
assay temperature during each acclimation experiment differ, they are followed
by different letters (P 0.05; ANOVA and Tukey's a
posteriori test).
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© The Company of Biologists Ltd 2003