PURIFICATION,CHARACTERIZATION AND STRUCTURE OF CM2Ph1,AN ANTIBACTERIAL PEPTIDE FROM Bombyx mori

Using HPLC we purified an antibacterial peptide named CMPhfrom the hemolymph ofpupae of silkworm （Bombyx mori） immunized with polyI:C. Amino acid composition analysisshowed that CMPhcontained 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 CMPhwas found to have inhibition effects invarying degrees on several bacterial strains. At a concentration of 0.35 μmol/L, CMPhcould inhibit the growth of 50% E. coli D31 strain. Some other antibacterial peptides were compared with CMPhin respect to their struc-tures and functions. Their homology was also discussed in this paper.