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.
|Number of pages||5|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - 1988 Jan 1|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology