. . "3"^^ . "Purification and characterization of antimicrobial peptides from fleshfly larvae haemolymph"@en . . "1" . . . . "Purification and characterization of antimicrobial peptides from fleshfly larvae haemolymph" . "RIV/60461373:22330/11:43892172" . . . . "432"^^ . . . . "Microbiological research is focused on solution of pathogen resistance problem. One of the potential solutions seems to be short cationic peptides naturally synthetized as a part of innate immunity. In our project larvae of the fleshly Neobellieria bullata were chosen as a source of these peptides. Several isolated fractions showed antimicrobial activity against bacteria and fungi. Tricine electrophoresis proved presence of low molecular peptide. MS analysis of antimicrobial active fractions determined molecular masses less than 10 kDa and the N-terminal sequencing gave us several sequences but not completed. The sequences do have very low similarity with peptides in the NCBI databases or with the database of antimicrobial peptides [2] and seem to be very unique" . . "Science and Technology against Microbial Pathogens. Research, Development and Evaluation" . "Neubauerov\u00E1, Tereza" . "Macek, Tom\u00E1\u0161" . . . "World Scientific Publishing Co. Pte. Ltd." . . "978-981-4354-85-1" . "Purification and characterization of antimicrobial peptides from fleshfly larvae haemolymph"@en . "22330" . . "RIV/60461373:22330/11:43892172!RIV12-MSM-22330___" . "P(GA522/09/1693), P(GD305/09/H008), Z(MSM6046137305)" . . "Singapore" . . "\u0160anda, Miloslav" . "5"^^ . . "Purification and characterization of antimicrobial peptides from fleshfly larvae haemolymph" . "[FCFD2E4EE307]" . "Neobellieria bullata; N-terminal sequencing; isolation; Antimicrobial peptides"@en . "Vob\u016Frka, Zden\u011Bk" . "225285" . "5"^^ . . "Microbiological research is focused on solution of pathogen resistance problem. One of the potential solutions seems to be short cationic peptides naturally synthetized as a part of innate immunity. In our project larvae of the fleshly Neobellieria bullata were chosen as a source of these peptides. Several isolated fractions showed antimicrobial activity against bacteria and fungi. Tricine electrophoresis proved presence of low molecular peptide. MS analysis of antimicrobial active fractions determined molecular masses less than 10 kDa and the N-terminal sequencing gave us several sequences but not completed. The sequences do have very low similarity with peptides in the NCBI databases or with the database of antimicrobial peptides [2] and seem to be very unique"@en . . "Mackov\u00E1, Martina" .