| Literature DB >> 3141410 |
T Nakamura1, H Furunaka, T Miyata, F Tokunaga, T Muta, S Iwanaga, M Niwa, T Takao, Y Shimonishi.
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.Entities:
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Year: 1988 PMID: 3141410
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157