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Preparation for the Monoclonal Antibody to the High Molecular Weight Proteins in the Myofibrils

Research Project

Project/Area Number 62560281
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 畜産化学
Research InstitutionNiigata University

Principal Investigator

SUZUKI Atsushi  Faculty of Agriculture, Niigata University: Professor, 農学部, 教授 (40018792)

Co-Investigator(Kenkyū-buntansha) IKEUCHI Yoshihide  Faculty of Agriculture, Niigata University: Assistant Professor, 農学部, 助教授 (90168112)
Project Period (FY) 1987 – 1988
Project Status Completed (Fiscal Year 1988)
Budget Amount *help
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1988: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1987: ¥1,500,000 (Direct Cost: ¥1,500,000)
KeywordsMuscle Protein / Myofibril / Meat Tenderization / Connectin / Z-nin / Monoclonal Antibody / ポリクロナル抗体 / 筋腹線維 / Z-nin / コネクチンのモノクロナル抗体
Research Abstract

Connection and Z-nin are high molecular weight proteins in the myofibrils. There are some questions about the role of both proteins on meat tenderization during postmortem storage.
1. The isolation of native connectih from rabbit skeletal muscle (L.dorsi) was carried out, and postmortem changes in native connection were studied quantitatively and qualitatively. On the basis of the amino acid composition and electrophoretic mobility on sds-polyacrylamide gel, it is ahown that the isolated protein was highly pure connectin. An increase of the extractability of native connectin from the muscle during storage was observed, and an electron microscopic study of the purified native connection indicates a qualitative change of connectin in the muscle during postmortem storage. If connection has some influence on meat tenderness, the quantitative and qualitative change of native connectin in the muscle are possibly one of the cause of meat tenderzation during cunditioning.
2. The polyclonal antibody to the native connectin was obtained from the balb/c mouse immunized with chicken connectin. The spleen cells of the balb/c mouse were fused with mouse myeloma cells (line NS-1) and the screening of the hybridoma cell with an ability to make antibody to connectin is now underway. From these results the procedure to obtain the monoclonal antibody to the native connectin seems to be almost established.
3. As to the Z-NIN, the isolation of it in a native state is impossible at present. So the ployclonal antibody to the denatured Z-NIN was prepared in our laboratory.

Report

(3 results)
  • 1988 Annual Research Report   Final Research Report Summary
  • 1987 Annual Research Report
  • Research Products

    (7 results)

All Other

All Publications (7 results)

  • [Publications] Atsushi Suzuki: Agricultural and Biological Chemistry. 52. 1439-1444 (1988)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] 鈴木敦士: "畜肉の熟成に関する研究の進歩ー解硬・軟化機構を中心にー、食品工業における科学・技術の進歩(III)" 光琳, 20 (1988)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Suzuki, Atsushi: "Postmortem Changes of Native Connectin in Rabbit Skeletal Muscle" Agricultural and Biological Chemistry. 52. 1439-1444 (1988)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Suzuki, Atsushi: Recent Studies on Meat Conditioning: in Advances in Food Science and Technology (III). Korin, 77-96 (1988)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Atsushi,Suzuki: Agriculturel and Biological Chemistry. 52. 1439-1444 (1988)

    • Related Report
      1988 Annual Research Report
  • [Publications] 鈴木敦士: "畜肉の熟成に関する研究の進歩-解硬・軟化機構を中心に-食品工業における科学・技術の進歩(III)" 光琳, 77-96 (1988)

    • Related Report
      1988 Annual Research Report
  • [Publications] Atsushi SUZUKI: Agricultural and Biological Chemistry. 52. (1988)

    • Related Report
      1987 Annual Research Report

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Published: 1987-04-01   Modified: 2016-04-21  

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