Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity

Shun Ichiro Kawabata, Fuminori Tokunaga, Yoshie Kugi, Shiho Motoyama, Yoshiki Miura, Michimasa Hirata, Sadaaki Iwanaga

研究成果: ジャーナルへの寄稿学術誌査読

77 被引用数 (Scopus)

抄録

A glycoprotein (M(r) = 43000) from horseshoe crab hemocytes with antimicrobial activity against Gram-negative bacteria was purified. The internal peptide sequences coincided exactly with the deduced amino acid sequence of a cDNA clone, designated limulus factor D, which was isolated by screening a hemocyte cDNA library with an anti-human plasminogen antibody. The open reading frame codes for a precursor of factor D of 394 amino acid residues, including an NH2-terminal signal sequence. The COOH-terminal domain of factor D has significant sequence homology with the catalytic domain of mammalian serine proteases, in particular with human tissue plasminogen activator (32% identity), except for the substitution of Ser of the active site triad to Gly. Factor D has a unique NH2-terminal domain with weak sequence homology with part of the mammalian interleukin-6 receptor α-chain. Factor D is likely to have an important role in host defense mechanisms.

本文言語英語
ページ(範囲)146-150
ページ数5
ジャーナルFEBS Letters
398
2-3
DOI
出版ステータス出版済み - 12月 2 1996

!!!All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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