Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages.
The microbicidal peptides, MCP-1 and MCP-2, of rabbit alveolar macrophages were purified by an improved procedure that employed preparative gel electrophoresis and high performance liquid chromatography. The peptides were arginine- and cystine-rich and lacked free sulfhydryl groups and detectable levels of carbohydrate. Complete sequence determinations revealed that MCP-1 differed from MCP-2 only by the substitution of arginine for leucine at residue 13 from the NH2 terminus and that the molecules were each single chain polypeptides of 33 amino acid residues containing three intramolecular disulfide bonds. The complete amino acid sequences of MCP-1 and MCP-2 are: (sequence in text)
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D002241:Carbohydrates / Q000032:analysis; D008168:Lung / Q000032:analysis*; D008264:Macrophages / Q000032:analysis*; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*; D011817:Rabbits; D013438:Sulfhydryl Compounds / Q000032:analysis
D023181:Antimicrobial Cationic Peptides; D002241:Carbohydrates; D011506:Proteins; D013438:Sulfhydryl Compounds