Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure

T. Nakamura, H. Furunaka, T. Miyata, F. Tokunaga, T. Muta, S. Iwanaga, M. Niwa, T. Takao, Y. Shimonishi

研究成果: Article

432 被引用数 (Scopus)

抄録

A cationic peptide, designated tachyplesin, was isolated from acid extracts of horseshoe crab (Tachypleus tridentatus) hemocyte debris. It consists of 17 residues and the structure determined by Edman degradation is: NH2-K-W-(C-F-R-V-(C-Y-R-G-I-C)-Y-R-R-C-)R-CONH2. The carboxyl-terminal end of this peptide was identified as arginine α-amide and the whole sequence including the α-amide was also confirmed by fast atom bombardment mass spectrometry, indicating a mass value of 2263. Tachyplesin inhibits growth of both Gram-negative and -positive bacteria at low concentrations and formed a complex with bacterial lipopolysaccharide. Tachyplesin seems likely to act as antimicrobial peptide for self-defense in the horseshoe crab against invading microorganisms.

本文言語English
ページ(範囲)16709-16713
ページ数5
ジャーナルJournal of Biological Chemistry
263
32
出版ステータスPublished - 1988 1 1

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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