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化学伝達物質としてのウシラクトフェリンの機能とその構造ユニットの解明

Research Project

Project/Area Number 03660289
Research Category

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

Allocation TypeSingle-year Grants
Research Field 畜産化学
Research InstitutionObihiro University of Agriculture and Veterinary Medicine

Principal Investigator

SHIMAZAKI Kei-ichi  OBIHIRO UNIV.OF AGR.& VET.MED.DEPT.OF BIORESOURCE CHEM.ASSOCIATE PROFESSOR, 畜産学部, 助教授 (10091547)

Project Period (FY) 1991 – 1993
Project Status Completed (Fiscal Year 1993)
Budget Amount *help
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1993: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1992: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1991: ¥1,300,000 (Direct Cost: ¥1,300,000)
Keywordslactoferrin / milk protein / monocyte / Trypanosoma / fragments / Trypanosoma cruzi / レセプタ-
Research Abstract

The C terminal half molecule (C lobe) of bovine lactoferrin was isolated by mild tryptic hydrolysis of lactoferrin followed by gel filtration and ion-exchange chromatography. The idntity of the fragment was established by determining its N terminal and C terminal amino acid sequences and comparing them with the amino acid sequence of intact lactoferrin.
The binding properties of intact lactoferrin and its fragments have been tested with bovine monocyte and with Trypanosoma cruzi. The specific binding with bovine lactoferrin was studied. Lactoferrin isolated from mature bovine milk by chromatographic method was used and labeled by ^<125>I-Bolton-Hunter reagent. From the binding assay, it was found that bovine milk lactoferrin could bind to bovine monocyte, specifically. And intact lactoferrin showed the binding ability to Trypanosoma cruzi (amastigote form). However, C terminal half molecule of bovine lactoferrin loses the binding capacity against Trypanosoma cruzi. Amastigote of Trypanosoma cruzi was obtained from mouse embryo fibroblast culture. The binding was studied by the method of the direct immunofluorescence test using FITC-labeled anti-bovine lactoferrin antibody (rabbit).

Report

(4 results)
  • 1993 Annual Research Report   Final Research Report Summary
  • 1992 Annual Research Report
  • 1991 Annual Research Report
  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] K.Shimazakiら10名: "Separation and characterization of the C-terminal-halfmolecule of bovine lactoferrin." J.Dairy Sci.76. 946-955 (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] 島崎敬一、清沢功: "ラクトフェリンその構造と機能" バイオサイエンスとインダストリー. 51. 25-27 (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] K.Shimazaki et al.: "Separation and characterization of C-terminal molecule of bovine lactoferrin" J.Dairy Sci.76(8). 946-955 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] K.Shimazaki and I.Kiyosawa: "Lactoferrin - Structure and Function" Bioscience and Industry. 51(1). 25-27 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] K.Shimazakiら10名: "Separation and characterization of the C-terminal-halfmolecule of bovine lactoferrin." J.Dairy Sci.76. 946-955 (1993)

    • Related Report
      1993 Annual Research Report
  • [Publications] 島崎敬一,清沢功: "ラクトフェリン -その構造と機能" バイオサイエンスとインダストリー. 51. 25-27 (1993)

    • Related Report
      1993 Annual Research Report
  • [Publications] 島崎 敬一: "Separation and Characterization of the C-terminal Half Molecule of Bovine Lactoferrin" J.Dairy Sci.76. (1993)

    • Related Report
      1992 Annual Research Report
  • [Publications] 島崎 敬一ほか: "Bovine monocyte separation and its interaction with lactoferrin: A preliminary study"

    • Related Report
      1991 Annual Research Report

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

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