Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils.
Six microbicidal peptides, NP-1, NP-2, NP-3a, NP-3b, NP-4, and NP-5, from rabbit peritoneal neutrophils were characterized. As a family, the peptides were 32-34 residues in length, were cystine- and arginine-rich, and each contained three intramolecular disulfide bonds. Within their sequences, the six peptides shared 11-residue positions, which included the six half-cystines contained in each peptide. NP-1 and NP-2 differed by a single residue and were identical in their respective sequences to MCP-1 and MCP-2, the peptide analogs from rabbit alveolar macrophages. NP-4 and NP-5 were homologous in 27 of their residues, but NP-3a and NP-3b shared little more than the 11-residue backbone common to all members of this peptide family.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D001483:Base Sequence; D001770:Blood Bactericidal Activity; D008264:Macrophages / Q000032:analysis; D008970:Molecular Weight; D009504:Neutrophils / Q000032:analysis*; D011506:Proteins / Q000032:analysis*; D011817:Rabbits; D014357:Trypsin / Q000378:metabolism
D000596:Amino Acids; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; D014357:Trypsin