1.
Adv Exp Med Biol
; 256: 273-85, 1990.
Article
in English
| MEDLINE
| ID: mdl-2109504
Subject(s)
Antimicrobial Cationic Peptides , DNA-Binding Proteins , Horseshoe Crabs/metabolism , Invertebrate Hormones/analysis , Lipopolysaccharides/analysis , Peptides, Cyclic , Peptides/analysis , Amino Acid Sequence , Amino Acids/analysis , Animals , Arthropod Proteins , Chemical Phenomena , Chemistry , Disulfides/analysis , Electrophoresis, Polyacrylamide Gel , Immunodiffusion , Invertebrate Hormones/isolation & purification , Mass Spectrometry , Molecular Sequence Data , Peptides/isolation & purification , Proteins/analysis
2.
J Biol Chem
; 263(32): 16709-13, 1988 Nov 15.
Article
in English
| MEDLINE
| ID: mdl-3141410
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.