Lipopolysaccharide-induced phosphorylation and partial amino acid sequence of a hemocyte protein in the silkworm, Bombyx mori.

DOI JASI Web Site 31 References
  • CHOI HONG KYU
    National Institute of Sericultural and Entomological Science
  • CHOI SU KYUNG
    National Institute of Sericultural and Entomological Science
  • TANIAI KIYOKO
    National Institute of Sericultural and Entomological Science
  • KADONO-OKUDA KEIKO
    National Institute of Sericultural and Entomological Science
  • KATO YUSUKE
    National Institute of Sericultural and Entomological Science
  • YAMAMOTO MASANORI
    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
  • SUGIYAMA MASAO
    National Institute of Sericultural and Entomological Science Present address: Hokko Chemical Industry Central Research Laboratories
  • MIYANOSHITA AKIHIRO
    National Institute of Sericultural and Entomological Science
  • DEBNATH NITISH C.
    National Institute of Sericultural and Entomological Science
  • ASAOKA AI
    National Institute of Sericultural and Entomological Science
  • YAMAKAWA MINORU
    National Institute of Sericultural and Entomological Science

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Other Title
  • 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
  • Lipopolysaccharide-induced phosphorylat

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Abstract

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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