Cloning and Expression of the<i>Momordica charantia</i>Trypsin Inhibitor II Gene in Silkworm by using a Baculovirus Vector

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  • SATO Shin-ichi
    Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
  • KAMEI Kaeko
    Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
  • TANIGUCHI Mai
    Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
  • SATO Hideki
    Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
  • TAKANO Ryo
    Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
  • MORI Hajime
    Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
  • ICHIDA Masatoshi
    Experimental Farms, Faculty of Textile Science, Kyoto Institute of Technology
  • HARA Saburo
    Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology

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  • Cloning and Expression of the Momordica charantia Trypsin Inhibitor II Gene in Silkworm by using a Baculovirus Vector.
  • Cloning and Expression of the Momordica charantia Trypsin Inhibitor 2 Gene in Silkworm by using a Baculovirus Vector

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  MCTI-II (Momordica charantia trypsin inhibitor II) isolated from bitter gourd (Momordica charantia LINN.) seeds is one of the serine protease inhibitors of the squash family. We cloned cDNA that encodes MCTI-II and constructed an expression system for MCTI-II by using a baculovirus vector. The recombinant baculovirus was inoculated to early fifth-instar larvae of the silkworm (strain: Shunrei×Shougetsu). Four days after infection, the hemolymph of silkworm larvae was collected and the recombinant protein was purified. Two kinds of expressed MCTI-II protein were obtained. An amino acid sequence analysis of the two proteins indicates that both were similar to the authentic inhibitor, except for the addition of a tripeptide derived from the vector at the N-terminus. One of the two inhibitors (MCTI-II A) resulted in a single PTH-amino acid in each Edman degradation cycle, while the other (MCTI-II B) resulted in two PTH-amino acids, suggesting the occurrence of cleavage of the reactive site. The inhibitory activities of MCTI-II expressed toward trypsin are examined in terms of the Ki value, these being 6.4×10-10 M for MCTI-II A and 5.2×10-10 M for MCTI-II B.<br>

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