Summary
The thermal characteristics of flight muscle and liver pyruvate kinase (PK) from the batMyotis lucifugus have been investigated in an attempt to understand the molecular strategies associated with hibernation. PKs of the hibernating and normothermic state differ in essentially five ways:
-
1.
Qualitative differences exist in the isozymic patterns (Fig. 1), with hibernator muscle PK having fewer types than normothermic muscle PK, and hibernator and normothermic liver PKs differing in the arrangement of bands, not total number.
-
2.
The specific activity of hibernator-PK is 1.5 to 2-fold higher than the normothermic enzyme (Figs. 2, 3, 5) which suggests the importance of this enzymic step at some point in the seasonal hibernating cycle of the bat.
-
3.
The PK found in a particular physiological state is that with the lowest thermal sensitivity (as indicated by reducedE a-values) over the temperature range characteristic of that state (Figs. 3, 5, 6, 7).
-
4.
Discontinuous Arrhenius plots are found for hibernator and normothermic tissue PKs, although the “critical temperature” (T c-value) is approximately 10°C lower for the hibernator enzyme (Figs. 3, 5).
-
5.
Temperature sensitivity is also noted in the binding of PEP and ADP to normothermic PK, although not in the hibernator enzyme (Figs. 4, 6, 7). The advantage of constant or fluctuating Q10-values is discussed in light of the biology of the bat.
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Abbreviations
- Ea :
-
activation energy
- FDP :
-
fructose-1,6-diphosphate
- PEP :
-
phosphoenol pyruvate
- PK :
-
pyruvate kinase
- Nl- andHL-:
-
normothermic and hibernator liver, respectively
- NM- andHM-:
-
normothermic and hibernator muscles, respectively
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Borgmann, A.I., Moon, T.W. Enzymes of the normothermic and hibernating bat,Myotis lucifugus: Temperature as a modulator of pyruvate kinase. J Comp Physiol B 107, 185–199 (1976). https://doi.org/10.1007/BF00691225
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DOI: https://doi.org/10.1007/BF00691225