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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.


Subject(s)
Anti-Bacterial Agents/isolation & purification , Antimicrobial Cationic Peptides , Blood Cells/analysis , Brachyura/analysis , DNA-Binding Proteins , Hemocytes/analysis , Peptides, Cyclic , Peptides/isolation & purification , Amino Acid Sequence , Amino Acids/analysis , Animals , Anti-Bacterial Agents/analysis , Gram-Negative Bacteria/drug effects , Gram-Positive Bacteria/drug effects , Immunodiffusion , Mass Spectrometry , Microbial Sensitivity Tests , Molecular Sequence Data , Peptides/analysis
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