Mol. Cells 2004; 17(2): 262-266
Published online January 1, 1970
© The Korean Society for Molecular and Cellular Biology
A cecropin-like antimicrobial peptide, Gm cecropin, was purified from hemolymph of larvae of the wax moth, Galleria mellonella, immunized against E. coli, and its antibacterial activity was examined in a radial diffusion assay. The molecular mass of Gm cecropin was 4,160.69 Da by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry analysis. The full-length cDNA of the Gm cecropin precursor was cloned by a combination of RT-PCR, based on the N-terminal sequence obtained by Edman degradation, and 5
Keywords Antimicrobial Peptide; cDNA; Cecropin; Galleria mellonella; Purification
Mol. Cells 2004; 17(2): 262-266
Published online April 30, 2004
Copyright © The Korean Society for Molecular and Cellular Biology.
Chong Han Kim, Joon Ha Lee, Iksoo Kim, Sook Jae Seo, Seok Min Son, Ki Young Lee, In Hee Lee
A cecropin-like antimicrobial peptide, Gm cecropin, was purified from hemolymph of larvae of the wax moth, Galleria mellonella, immunized against E. coli, and its antibacterial activity was examined in a radial diffusion assay. The molecular mass of Gm cecropin was 4,160.69 Da by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry analysis. The full-length cDNA of the Gm cecropin precursor was cloned by a combination of RT-PCR, based on the N-terminal sequence obtained by Edman degradation, and 5
Keywords: Antimicrobial Peptide, cDNA, Cecropin, Galleria mellonella, Purification