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Research on the structure and function of antihemorrhagic factor

Research Project

Project/Area Number 05660103
Research Category

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

Allocation TypeSingle-year Grants
Research Field 応用微生物学・応用生物化学
Research InstitutionUniversity of The Ryukyus

Principal Investigator

YONAHA Kazuo  Univ. of The Ryukyus, Agicuture, Assoc. Prof., 農学部, 助教授 (50101184)

Project Period (FY) 1993 – 1994
Project Status Completed (Fiscal Year 1994)
Budget Amount *help
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1994: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1993: ¥1,300,000 (Direct Cost: ¥1,300,000)
Keywordssnake venom / hemorrhagic / antihemorrhagic / protein / evolution / structure / mongoose / mRNA / cDNA / 一次構造
Research Abstract

This research has been taken by aiming at the development of a novel antitoxin with antihemorrhagic factor of mongoose. Three antihemorrhagic factors of mongoose were purified and characterized in this research. The three factors, AHF1, AHF2, and AHF3, are glycoproteins of monomer structure. AHF1 completely inhibited the hemorrhagic activity of HR2b, hemorrahgic factor of Habu snake. The antihemorrhagic factor formed a complex with the hemorrahgic facor. No alteration in the primary or secondary structures of both factors was demonstrated before and after incubation of both factors.
The three antihemorrhagic factors are composed of about 600 amino acids of similar composition. AHF1 and AHF2 were of the same amino terminal amino acid sequence, but AHF3 showed different sequence, though high homology was found between AHF3 and the other two antihemorrhagic factors. The amino acid sequence of AHF1 covering 75.9% of whole sequence of human alpha1B-glycoprotein (alpha1B-G) showed 46.1% identity with the sequece of alpha1BG.These results suggest for the antihemorrhagic factor to be a homologous protein with human alpha1B-G and therefore a supergene family of immunoglobulin, and the different ancestral proteins for the antihemorrhagic factors of mammals and repitiles.
The total RNA was successfully prepared from the liver of mongoose, and mRNA was isolated from the RNA preparation. The cDNA library containing 10^<10>/ml independent phage particle was constructed.

Report

(3 results)
  • 1994 Annual Research Report   Final Research Report Summary
  • 1993 Annual Research Report
  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] Zhi-Aing Qi: "Characterization of the antihemorrhagic factor of mongoose(Herpestes edwordsii)" Toxicon. 32. 1459-1469 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Zhi-Aing Qi: "Isolation of peptides homelogeus to domains of human HB-glycoprotein from a mongoose antihemonhogic factor" Toxicon. 33. 241-245 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Zhi-Qing Qi, Kazuo Yonaha, Yasuhiro Tomihara and Seizen Toyama: "Characterization of the antihemorrhagic factorof mongoose (Herpestes edwardsii)" Toxicon. 32 (11). 1459-1469 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Zhi-Qing Qi, Kazuo Yonaha, Yasuhiro Tomihara and Seizen Toyama: "Isolation of peptides homologous to domains of human alpha1B-glycoprotein from a mongoose antihemorrhagioc factor" Toxicon. 33 (2). 241-245 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Zhi-Qing Qi: "Characterigation of anfihemorrhagic Ractors of mongoose(Herpestes edwardsii)" Toxicon. 32. 1459-1469 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] Zhi-Qing Qi: "Isolation of homologous peptides to domains of human α1B-glycoprotein from a mongoose antihemorrhagic factor" Toxicon. 33(印刷中). (1995)

    • Related Report
      1994 Annual Research Report

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Published: 1993-04-01   Modified: 2016-04-21  

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