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Differences in the Thermal Stability of Acclimation Temperature-Associated Types of Carp Myosin and Its Rod on Differential Scanning Calorimetry



Differences in the Thermal Stability of Acclimation Temperature-Associated Types of Carp Myosin and Its Rod on Differential Scanning Calorimetry



Biochemistry. 34(9): 3114-3120



Differential scanning calorimetry (DSC) was employed for studying the thermal unfolding of myosin and its rod part prepared from carp acclimated to 10 and 30 degree C. Differences in the thermal stability reflecting structural properties were clearly demonstrated by the DSC data obtained at pH 8.0 in 0.6 M KCl for the two types of carp myosin and rod. The transition temperatures on myosin and rod given by the major peaks for the 10 degree C-acclimated carp were 33.9 and 47.4 degree C and 33.0 and 44.0 degree C, respectively, assuming two endotherms for this type. Since the shape of the first peaks at 33.9 and 33.0 degree C was not symmetrical, two peaks having similar transition temperatures overlapped in this temperature range. When the data were analyzed using three endotherms, the three transition temperatures obtained for myosin and rod were 32.8, 34.9, and 47.4 degree C and 32.9, 33.4, and 44.1 degree C, respectively. Thus, the position of the first peak for the 10 degree C-acclimated carp myosin did not change even after removal of the large subfragment-1 part, but the transition of the second peak shifted to a lower temperature by about 3 degree C. The myosin and rod from carp acclimated to 30 degree C showed three distinct peaks at 35.9, 39.7, and 49.1 degree C and 34.5, 39.7, and 46.7 degree C, respectively. The position of the largest peak for myosin remained unchanged, and the shift of the peak position of the highest temperature was about 3 degree C, as obtained for the 10 degree C-acclimated carp. The calorimetric enthalpies were 86, 146, and 69 kcal/mol for the 10 degree C-acclimated rod and 95, 115, and 159 kcal/mol for the 30 degree C-acclimated rod, respectively, in the order of the above endotherms. The DSC runs at pH 6.5 also gave similar results. Thermal unfolding responsible for these endotherms was mostly explained by melting of alpha-helices which could be determined by far-ultraviolet CD spectroscopy.

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Accession: 008466943

Download citation: RISBibTeXText

PMID: 7893723

DOI: 10.1021/bi00009a043


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