One antimicrobial peptide was isolated and purified to 5.50-fold from the crude lysate of immunised Aedes caspius larvae by (NH4)2SO4 fractionation, ion-exchange chromatography, and reverse-phase high performance liquid chromatography (HPLC). The peptide, named ACAm, was found to be heat stable below 80 °C and exhibited strong antimicrobial activities against Gram-positive and Gram-negative bacteria as well as against peptidoglycans and lipopolysaccharides of bacterial cell walls. The estimated molecular weight of ACAm by sodium dodecyl sulphate polyacrylamide gel (SDS-PAGE), under non-reducing conditions, was 4 kDa. Using isoelectric focusing (IEF), ACAmexhibited pI in basic pH (8.4) belonging to cationic peptides.
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Vol. 24 • No. 1