Purification of sarcotoxin II, antibacterial proteins of Sarcophaga peregrina (flesh fly) larvae

Biochemistry. 1987 Jan 13;26(1):226-30. doi: 10.1021/bi00375a030.


Three antibacterial proteins with almost identical primary structures termed sarcotoxin IIA, IIB, and IIC were purified to homogeneity from the hemolymph of third instar larvae of Sarcophaga peregrina. The molecular masses of these proteins were about 24,000. These proteins were found to have common antigenicity, and antibody against sarcotoxin IIA cross-reacted with sarcotoxin IIB and IIC. Radioimmunoassay using this antibody showed that these proteins are induced in the hemolymph in response to injury of the larval body wall.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Anti-Infective Agents / isolation & purification*
  • Diptera*
  • Hemolymph
  • Immunodiffusion
  • Insect Hormones / isolation & purification*
  • Insect Proteins*
  • Larva
  • Molecular Weight
  • Radioimmunoassay


  • Amino Acids
  • Anti-Infective Agents
  • Insect Hormones
  • Insect Proteins
  • sarcotoxin IIA protein, Sarcophaga peregrina
  • sarcotoxin IIB protein, Sarcophaga peregrina
  • sarcotoxin IIC protein, Sacrophaga peregrina