Abstract
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: (formula; see text) The carboxyl-terminal end of this peptide was identified as arginine alpha-amide, and the whole sequence including the alpha-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.
Highlights
From theDepartment of Bwlogy, Faculty of Science and the $Department of Molecular Biology, Graduate School of Medical Science, Kyushu University 33, Fukmka 812,Japan
This paper deals with the isolation and tridentatus) hemocyte debris
The hemocytes circulating in limulus hemolymph are highly
Summary
From theDepartment of Bwlogy, Faculty of Science and the $Department of Molecular Biology, Graduate School of Medical Science, Kyushu University 33, Fukmka 812,Japan
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