Purification and characterization of a diptericin homologue from Sarcophaga peregrina (flesh fly).
A protein with a molecular mass of 8 kDa was found to be synthesized specifically when the fat-body from injured Sarcophaga peregrina larvae was cultured in vitro. This protein was purified from the haemolymph of the injured larvae to near-homogeneity. Partial amino acid sequencing revealed that this protein is a diptericin homologue. It showed bactericidal activity on growing, but not resting Escherichia coli cells. E. coli cells become elongated on treatment with this protein.
Ishikawa
M
M
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Kubo
T
T
Natori
S
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology; D004175:Diptera / Q000737:chemistry* / Q000378:metabolism; D029721:Drosophila Proteins; D005216:Fat Body / Q000737:chemistry / Q000378:metabolism; D006458:Hemolymph / Q000737:chemistry; D007301:Insect Hormones / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D019476:Insect Proteins; D007814:Larva / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D000890:Anti-Infective Agents; C054756:DptA protein, Drosophila; D029721:Drosophila Proteins; D007301:Insect Hormones; D019476:Insect Proteins