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Species differences in myosin stability warrant caution in cross-species models; leaves open cardiac myosin implications in variable thermal conditions.
The thermal stability of myosin of carp was compared with that of rabbit using differential scanning calorimetry (DSC), circular dichroism (CD), and fluorescence intensity. A structural change of myosin began at 40°C for rabbit and at 30°C for carp. So, carp myosin was more unstable than that of rabbit. Additionally, although rabbit myosin unfolded in a single-peaked transition, carp myosin unfolded in double-peaked transitions. The change corresponding to this first transition occurs in both subfragment-1 and light meromyosin (LMM), as judged from the CD measurements of myosin fragments. This suggests that the instability of carp myosin is reflected in its subfragment-1 and LMM.
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Ogawa et al. (1994) studied this question.
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