Fig. 1. Fractionation of hemolymph extracts from the immunized larvae by cation exchange chromatography. (A) Profile of cation exchange chromatography using HiTrap SP HP column with linear gradient of 0 - 80% 1.5M NaCl as the first step purification. The peak containing antibacterial activity is indicated with an arrow. (B) Antibacterial activity of fractions eluted form the cation exchange column by agar well diffusion assay (C) Tricine SDS-PAGE analysis of eluted fractions containing antibacterial activity.
Fig. 2. Final purification of antimicrobial peptides by gel permeation chromatography. (A) Profile of superdex peptide gel permeation chromatography as the final purification. The peaks containing strongest antibacterial activity are indicated with arrows. (B) Agar well diffusion assay of fractions 19 ~30 collected form the superdex peptide column. (C) Tricine SDS-PAGE analysis of fractions 18 ~ 28 containing antibacterial activity.
Table 1. N-terminal amino acid sequences of purifed peptides
Table 2. Antimicrobial activity of purifed cecropin and moricin
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피인용 문헌
- Functional analysis of the antioxidant activity of immune-challenged Bombyx mori hemolymph extracts in the human epithelial Caco-2 cell line vol.40, pp.1, 2018, https://doi.org/10.7852/ijie.2020.40.1.16