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Using HPLC we purified an antibacterial peptide named CM_2Ph_1 from the hemolymph ofpupae of silkworm (Bombyx mori) immunized with polyI:C. Amino acid composition analysisshowed that CM_2Ph_1 contained 16 kinds of amino acids. Its primary structure determined bythe automatic Edman degradation method is GNFFKDLEKMGQRVRDAVISAAPAVDTLAKA-KALGQ. Its C-terminal residue was assumed to be Gln with a blocking α-carboxylamide bycarboxypeptidases analysis. The purified CM_2Ph_1 was found to have inhibition effects invarying degrees on several bacterial strains. At a concentration of 0.35 μmol/L, CM_2Ph_1could inhibit the growth of 50% E. coli D31 strain. Some other antibacterial peptides were compared with CM_2Ph_1 in respect to their struc-tures and functions. Their homology was also discussed in this paper.
Using HPLC we purified an antibacterial peptide named CM_2Ph_1 from the hemolymph of pupae of silkworm (Bombyx mori) immunized with polyI: C. Amino acid composition analysisshowed that CM_2Ph_1 contained 16 kinds of amino acids. Its primary structure determined by the automatic Edman degradation method is GNFFKDLEKMGQRVRDAVISAAPAVDTLAKA- KALGQ. Its C-terminal residue was assumed to be Gln with a blocking α-carboxylamide bycarboxypeptidases analysis. The purified CM_2Ph_1 was found to have inhibition effects invarying degrees on several bacterial strains. At a concentration of 0.35 μmol / L, CM_2Ph_1could inhibit the growth of 50% E. coli D31 strain. Some other antibacterial peptides were compared with CM_2Ph_1 in respect to their struc-tures and functions. Their homology was also discussed in this paper.