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|Title:||Induction, purification and characterization of an antibacterial peptide scolopendrin I from the venom of centipede Scolopendra subspinipes mutilans|
|Keywords:||Centipede;Scolopendra subspinipes mutilans;Antibacterial peptide;Scolopendrin I;Venom;E. coli K12D31;Induction;Hemolytic activity;Agglutination activity|
|Abstract:||The crude venom of the centipede Scolopendra subspinipes mutilans, injected with Escherichia coli K₁₂D₃₁ for 3-4 days showed broad-spectrum antimicrobial activity against Gram-positive, Gram-negative bacteria and fungi. It showed good antibacterial activity against E. coli K₁₂D₃₁ at different temperatures, pH, and ionic strengths. The crude venom was heated at 100°C for 30 min, centrifuged at 10,000 rpm for 30 min at 4°C and the supernatants were obtained, from which an antibacterial fraction having a molecular mass of 3000-5000 Da, was further separated by ultrafiltration. A homogeneous antibacterial peptide named scolopendrin I, having a molecular mass of 4,498 Da, was isolated using cation-exchange chromatography and two steps of reverse-phase high performance liquid chromatography (RP-HPLC). Scolopendrin I did not show any hemolytic and agglutination activities at the concentration below 30 μM.|
|Appears in Collections:||IJBB Vol.43(2) [April 2006]|
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