カイコの糸状菌プロテアーゼインヒビター (FPI-F) のcDNAクローニングと発現

  • 伊藤 雅信
    Department of Applied Biology, Kyoto Institute of Technology
  • 竹中 徹
    Department of Applied Biology, Kyoto Institute of Technology
  • 芦刈 俊彦
    Plant Biotechnology Laboratory, Institute for Fundamental Research, Suntory Limited
  • 江口 正治
    Department of Applied Biology, Kyoto Institute of Technology

書誌事項

タイトル別名
  • cDNA cloning and expression of a novel type protease inhibitor (FPI-F) from the silkworm, Bombyx mori.
  • c DNA cloning and expression of a novel

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抄録

We isolated and analyzed a cDNA encoding the fungal protease specific inhibitor-F (FPI-F) of the silkworm, Bombyx mori. The cDNA contained 410 nucleotides including a 15 adenine tract. The deduced amino acid sequence showed an open reading frame encoding 77 amino acid residues which had a highly hydrophobic amino terminal signal peptide containing 22 amino acids. On the whole, we could not find homologous sequences to FPI-F by surveying protein and DNA databases, which suggests that FPI-F is a novel molecule of protease inhibitor. RNA blot analysis revealed that the FPI-F gene is expressed in several tissues as 0.45kb transcript. The highest expression was detected in the integument. This result is significant, since the integument is the first barrier for invading fungi. Considerable amounts of transcript were seen in the silk gland and fat body of the silkworm.

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