Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure.
1988; Elsevier BV; Volume: 263; Issue: 32 Linguagem: Inglês
10.1016/s0021-9258(18)37448-9
ISSN1083-351X
AutoresTakanori Nakamura, Hiromi Furunaka, Toshiyuki Miyata, Fuminori Tokunaga, Tsuyoshi Muta, Shiroh Iwanaga, Makoto Niwa, Toshifumi Takao, Yasutsugu Shimonishi,
Tópico(s)Biochemical and Structural Characterization
ResumoA 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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