2003 Fiscal Year Final Research Report Summary
The study on the mechanism of solubilization of myofibrillar proteins in water
| Project/Area Number |
13460115
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Zootechnical science/Grassland science
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| Research Institution | Hokkaido University |
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Principal Investigator |
HATTORI Akihito Hokkaido University, Graduate School of Agriculture, Professor, 大学院・農学研究科, 教授 (50125027)
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| Co-Investigator(Kenkyū-buntansha) |
NISHIMURA Takanori Hokkaido University, Graduate School of Agriculture, Associate Professor, 大学院・農学研究科, 助教授 (10237729)
WAKAMATSU Jun-ichi Hokkaido University, Graduate School of Agriculture, Assistant Professor, 大学院・農学研究科, 助手 (30344493)
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| Project Period (FY) |
2001 – 2003
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| Keywords | Water-soluble myofibrillar proteins / myosin / a low ionic strength neutralsolution / L-histidine / Myosin monomer / thick filament / length of myosin rod |
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| Research Abstract |
We have created an alternative solubilizing method that has resulted in solubilizing more than 80% of chicken breast muscle myofibrillar proteins in water The purpose of this study is to determine the solubilization mechanism of myosin in a low ionic strength solution. We have shown that myosin, a major myofibrillar protein, prepared from chicken skeletal muscle can also be solubilized in the same manner, and it is essential to maintain myosin suspensions at a neutral pH with L-histidine(L-His) and at a low ionic strength. The results from the SDS-PAGE with EDC reactions have shown water-soluble myosin was morphologically different from native myosin under the same physiological and high ionic strength conditions. This suggests that water-soluble myosin exists as neither a monomer nor a thick filament Electron microscopy have also showed that in neutral and low ionic strength solutions with L-His, the water-soluble myosin molecules exist in two forms : separated monomers and very thin filament-like structures. It was further determined that water-soluble myosin has longer rods than native myosin which suggested that the addition of L-His created structural changes in rod length. We conclude that this structural change made myosin solubilize in low ionic strength solutions.
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