Proteolytic degradation of muscllarr proteins of red sea bream by using immuno-electron mycroscope and immunoblot analysis
| Project/Area Number |
10660198
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Fisheries chemistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
HARA Kenji Nagasaki University, Faculty of Fisheries, Professor, 水産学部, 教授 (10039737)
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| Co-Investigator(Kenkyū-buntansha) |
TACHIBANA Katsuyasu Nagasaki University, Faculty of Fisheries, Associate Professor, 水産学部, 助教授 (20171712)
ISHIHARA Tadashi Nagasaki University, Faculty of Fisheries, Professor, 水産学部, 教授 (40039722)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1999: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1998: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | Red sea bream Muscle / Autolysis / Protease / Myofibrillar Proteins / Protease Inhibitor / 筋原繊維タンパク質 |
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| Research Abstract |
We examined the degradation of post-mortem myofibrillar proteins (myosin heavy chain, α-actinin, β-connectin and troponin I) of red sea bream Pagrus major in relation with internal proteases by using specific protease inhibitors. These proteins were considerably hydrolyzed with internal proteinase(s) at 25℃ for 3 days. We confirmed that Cathepsin L which is cysteine protease in skeretal muscle was inhibited by E-64, specific cysteine protease inhibitor, injected to duct of Cuvie. Degradation of myosin HC and β-connectin were strongly inhibited by serine protease inhibitor (leupeptin and DFP). It was suggested that myosin HC is hydrolyzed by serine protease (may be MBP, myosin binding serine proteinase). Limited degradation of α-actinin was inhibited by cysteine protease inhibitor(E-64). The findings suggests that α-actinin is degraded by cathepsins B, L or S. Hydrolysis of tropomyosin and troponin I were mainly inhibited by serine protease inhibitors (leupeptin and DFP) and secondly inhibited by cysteine protease inhibitor(E-64). It is suggested that these proteins are hydrolyzed by MBP and the cathepsins.
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Report
(3 results)
Research Products
(3 results)
