Heat-induced structural changes and aggregation of walleye pollack myosin in the light meromyosin region.

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  • HIGUCHI TOMOYUKI
    Laboratory of Biochemistry and Biotechnology, Graduate School of Fisheries Sciences, Hokkaido University
  • OJIMA TAKAO
    Laboratory of Biochemistry and Biotechnology, Graduate School of Fisheries Sciences, Hokkaido University
  • NISHITA KIYOYOSHI
    Laboratory of Biochemistry and Biotechnology, Graduate School of Fisheries Sciences, Hokkaido University

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Heat-induced structural changes and aggregation properties of walleye pollack myosin, light meromyosin (LMM) and heavy meromyosin (HMM) were investigated. According to the circular dichroism (CD) measurement, the α-helix content of the pollack myosin and LMM were estimated to be 72% and 90% at 5°C but decreased to 22% and 21% by increasing the temperature to 60°C with two transitions at 35°C and 50°C, respectively. In contrast, that of HMM decreased gradually from 37% to 33% by increasing the temperature from 5°C to 40°C, and decreased steeply to 20% above 50°C. These results indicate that the decrease in the α-helix content in the myosin molecule upon heating was attributable mainly to the decrease in the α-helix content in the LMM region. In contrast, 1-anilinonaphthalene-8-sulfonate (ANS) fluorescence and light scattering intensity of both myosin and HMM were remarkably increased above 25°C and 35°C, respectively, while those of LMM showed only a slight change even above 60°C. Although LMM alone formed no aggregates detectable by the light scattering measurement, it formed coprecipitates with myosin but not with HMM upon heating at 40°C for 10 min. These facts suggest that LMM bind to the LMM region of the myosin. Further, it was found that myosin gel formed in a test tube by the same heating conditions was significantly weakened by coexistence of LMM. These results suggest that the association of the LMM region of myosin molecules is essential for the heat-induced gelation of myosin.

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