Isolation, identification and synthesis of locustamyotropin (Lom-MT), a novel biologically active insect peptide

Peptides. 1990 May-Jun;11(3):427-33. doi: 10.1016/0196-9781(90)90038-7.

Abstract

A peptide that stimulates the spontaneous contractions of the hindgut of Leucophaea maderae has been purified from extracts of brain-corpora cardiaca/corpora allata-subesophageal ganglion complexes of 9000 adult Locusta migratoria and was designated locustamyotropin or Lom-MT. The primary structure of this 12 residue peptide has been determined Gly-Ala-Val-Pro-Ala-Ala-Gln-Phe-Ser-Pro-Arg-Leu-NH2. The C-terminal sequence (Phe-Ser-Pro-Arg-Leu-NH2) is identical to the C-terminal pentapeptide of the pheromone biosynthesis activating neuropeptide, recently isolated from Heliothis zea, and is also similar to the C-terminal of leucopyrokinin of Leucophaea. Synthetic Lom-MT showed biological as well as chemical characteristics, indistinguishable from those of native Lom-MT. In locust preparations, Lom-MT provoked an increase in frequency, amplitude and tonus of contractions of the oviduct, but was inactive in the same conditions on the locust hindgut preparation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Aminopeptidases
  • Animals
  • Biological Assay
  • CD13 Antigens
  • Chromatography, High Pressure Liquid
  • Grasshoppers / analysis*
  • Molecular Sequence Data
  • Neuropeptides / analysis
  • Neuropeptides / chemical synthesis
  • Neuropeptides / isolation & purification*
  • Sequence Homology, Nucleic Acid

Substances

  • Neuropeptides
  • locustamyotropin
  • Aminopeptidases
  • CD13 Antigens