Scanning Calorimetric Studies on Thermal Denaturation of Myosin and Its Subfragments
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概要
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Myosin and its subfragments were prepared from rabbit skeletal muscle and studied in a differential scanning calorimeter. The characteristics of the observed endotherms were studied as a function of pH and salt concentration. An analysis of the DSC profiles for myosin and its subfragments in 0.6M KCl enabled the assignment of three components of the endotherms for myosin in solution to structural transitions in the head (globular) and tail (coiled-coil) regions of the molecule. However, large shifts for the Tm values as well as the reduction of the number of transitions were observed upon changing pH and salt concentration of the basal media. Comparison of the calorimetric behavior of myosin and its helical subfragments at a high salt concentration (0.6M KCl) with those at a low salt concentration (0.1M KCl) showed them to be remarkably different, suggesting that the DSC profiles at low salt concentrations are represented by the filaments of myosin and paracrystals of helical subfragments, wherein intermolecular interactions stabilize organized molecules through their self-associating properties.
- 社団法人 日本農芸化学会の論文
著者
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Yasui Tsutomu
Department Of Animal Science Faculty Of Agriculture Hokkaido Unviersity
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SAMEJIMA Kunihiko
Department of Dairy Science, The College of Dairying
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ISHIOROSHI Makoto
Department of Animal Science, Faculty of Agriculture, Hokkaido University
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