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In Vitro Motility Assays of Myosin Blocked with Modifiers

Research Project

Project/Area Number 03454555
Research Category

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

Allocation TypeSingle-year Grants
Research Field 分子遺伝学・分子生理学
Research InstitutionAsahikawa Medical College

Principal Investigator

HIRATSUKA Toshiaki  Asahikawa Medical College Chemistry Associate Professor, 医学部, 助教授 (30041825)

Project Period (FY) 1991 – 1992
Project Status Completed (Fiscal Year 1992)
Budget Amount *help
¥5,900,000 (Direct Cost: ¥5,900,000)
Fiscal Year 1992: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1991: ¥4,300,000 (Direct Cost: ¥4,300,000)
KeywordsMyosin / Muscle contraction / Motility assays
Research Abstract

In Vitro Motility Assays of Myosin Blocked with Modifiers
The effects of the chemical modifications of myosin's reactive cysteines on actomyosin adenosine triphosphatase(ATPase) activities and sliding patterns in the in vitro motility assays were examined. The two types of modifications studied were 5-(iodoacetamido)fluorescein labeling of SH1(Cys-707) and 2-(4'- maleimidylanilino)naphthalene-6-sulfonic acid labeling of SH2(Cys-697). Each type of modified myosin inhibited the sliding of actin in motility assays. However, the possibility that the observed inhibition of the sliding of actin induced by modified myosins may result from structural perturbation caused by bulky modifiers cannot be ruled out by the present work.

Report

(3 results)
  • 1992 Annual Research Report   Final Research Report Summary
  • 1991 Annual Research Report
  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] Toshiaki Hiratsuka: "Specific Labeling of Cys-707 in Myosin ATPase with a Fluorophore Directly Linked to the Sulfur Atom to Monitor Structural Changes in the Immediate Vicinity of the Thiol" Journal of Biological Chemistry. (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Toshiaki Hiratsuka: "Reactive Thiols Cys-707(SH1) and Cys-697(SH2) in Myoshin ATPase Behave in Opposite Manner upon Binding and Hydrolysis of ATP" Journal of Biological Chemistry. (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Toshiaki Hiratsuka: "Specific Labeling of Cys-707 in Myosin ATPase with a Fluorophore Directly Linked to the Sulfur Atom to Monitor Structural in the Immediate Vicinity of the Thiol" J.Biol.Chem. (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Toshiaki Hiratsuka: "Reactive Thiols Cys-707(SH1) and Cys-697(SH2) in Myosin ATPase Behave in Opposite Manner upon Binding and Hydolysis of ATP" J.Biol.Chem. (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Toshiaki Hiratsuka: "Specific Labeling of Cys-707 in Myosin ATPase with a Fluorophore Directly Linked to the Sulfur Atom to Monitor Structural Changes in the Immediate Vicinity of the Thiol" Journal of Biological Chemistry. (1993)

    • Related Report
      1992 Annual Research Report
  • [Publications] Toshiaki Hiratsuka: "Reactive Thiols Cys-707(SHI)and Cys-697(SH2)in Myosin ATPase Behave in Opposite Manner upon Binding and Hydrolysis of ATP" Journal of Biological Chemistry. (1993)

    • Related Report
      1992 Annual Research Report

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Published: 1991-04-01   Modified: 2016-04-21  

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