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

      The Journal of Biological Chemistry
      Amino Acid Sequence, Amino Acids, analysis, Animals, Anti-Bacterial Agents, isolation & purification, Antimicrobial Cationic Peptides, Blood Cells, Brachyura, DNA-Binding Proteins, Gram-Negative Bacteria, drug effects, Gram-Positive Bacteria, Hemocytes, Immunodiffusion, Mass Spectrometry, Microbial Sensitivity Tests, Molecular Sequence Data, Peptides, Peptides, Cyclic

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          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.

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