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. 1992 Oct 15;287(Pt 2):573–578. doi: 10.1042/bj2870573

Purification and characterization of a diptericin homologue from Sarcophaga peregrina (flesh fly).

M Ishikawa 1, T Kubo 1, S Natori 1
PMCID: PMC1133203  PMID: 1445217

Abstract

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.

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Selected References

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