カイコ血球タンパク質のリポポリサッカライドによるリン酸化の誘導と部分アミノ酸配列

  • 崔 洪圭
    National Institute of Sericultural and Entomological Science
  • 崔 秀景
    National Institute of Sericultural and Entomological Science
  • 谷合 幹代子
    National Institute of Sericultural and Entomological Science
  • 門野 敬子
    National Institute of Sericultural and Entomological Science
  • 加藤 祐輔
    National Institute of Sericultural and Entomological Science
  • 山本 眞則
    National Institute of Sericultural and Entomological Science
  • CHOWDHURY SUBRATA
    National Institute of Sericultural and Entomological Science
  • XU JINHUA
    National Institute of Sericultural and Entomological Science
  • 杉山 正夫
    National Institute of Sericultural and Entomological Science Present address: Hokko Chemical Industry Central Research Laboratories
  • 宮ノ下 明大
    National Institute of Sericultural and Entomological Science
  • DEBNATH NITISH C.
    National Institute of Sericultural and Entomological Science
  • 朝岡 愛
    National Institute of Sericultural and Entomological Science
  • 山川 稔
    National Institute of Sericultural and Entomological Science

書誌事項

タイトル別名
  • Lipopolysaccharide-induced phosphorylation and partial amino acid sequence of a hemocyte protein in the silkworm, Bombyx mori.
  • Lipopolysaccharide-induced phosphorylat

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抄録

Some hemocyte proteins from the silkworm, Bombyx mori, were found to be phosphorylated when isolated hemocytes were incubated with [32P] orthophosphate in the presence of bacterial lipopolysaccharide (LPS). On the other hand, the LPS-induced phosphorylation was not observed in BmN4 cells, a cell line originated from B. mori embryo, suggesting that the phosphorylation occurs tissue-specifically. One of the phosphorylated hemocyte proteins having molecular weight of 37, 000 was purified and digested with V8 protease or lysylendopeptidase. The amino acid sequence of the proteolytic fragments was determined and compared with those of other reported proteins. The results showed that the partial amino acid sequence of the 37kDa protein has 98% identity with that of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Drosophila melanogaster, suggesting that the 37kDa protein is related to GAPDH and involved in the self-defense system in B. mori.

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