| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Outline of Final Research Achievements |
High hydrostatic pressure induces a weakening of intramuscular connective tissue, which is mainly composed of collagen. Decorin, a small proteoglycan, binds to and stabilizes collagen fibrils.It has been suggested that the weakening of intramuscular connective tissue may result from alteration of the decorin-collagen interaction due to structural changes of the decorin molecule. In the present study, decorin was isolated and purified from bovine skeletal muscle, and then the molecular structure of the isolated decorin under high pressure was investigated. The results were following: (1) Degradation of core protein and GAG chain of the isolated decorin was not revealed by high pressure. (2) Measurements of fluorescence spectra and surface hydrophobicity indicated that the tertiary structure of decorin was altered reversibly under high pressure up to 400 MPa. (3) High pressure did not affect surface SH-group content of decorin molecules.
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