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Proteolytic degradation of muscllarr proteins of red sea bream by using immuno-electron mycroscope and immunoblot analysis

Research Project

Project/Area Number 10660198
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Fisheries chemistry
Research InstitutionNagasaki University

Principal Investigator

HARA Kenji  Nagasaki University, Faculty of Fisheries, Professor, 水産学部, 教授 (10039737)

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)
Project Period (FY) 1998 – 1999
Project Status Completed (Fiscal Year 1999)
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)
KeywordsRed sea bream Muscle / Autolysis / Protease / Myofibrillar Proteins / Protease Inhibitor / 筋原繊維タンパク質
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.

Report

(3 results)
  • 1999 Annual Research Report   Final Research Report Summary
  • 1998 Annual Research Report
  • Research Products

    (3 results)

All Other

All Publications (3 results)

  • [Publications] Kenji Hara et al.: "Proteolytic Degradation of Fish Myofibrillar Proteins by Internal Proteases"Proc. 9th JSPS Joint Sem. Mar. Fish. Sci.. 279-309 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] K.Hara, H.Pangkey, M.Kurihara, K.Tachibana, M.-J.Cao, K.Osatomi and T.Ishihara: "Proteolytic Degradation of Fish Myofibrillar Proteins by Internal Proteases"Proc.9th JSPS Joint Sem. Mar. Fish. Sci.. 299-309 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Kenji Hara et al: "Proteolytic Degradation of Fish Myofibrillar Proieins by Internal Proieases"Proc.9th JSPS Joint Sem.Mar.Fish.Sci.. 299-309 (1999)

    • Related Report
      1999 Annual Research Report

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Published: 1998-04-01   Modified: 2016-04-21  

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