Primary sequence analysis by fast atom bombardment mass spectrometry of a peptide with adipokinetic activity from the corpora cardiaca of the cricket Gryllus bimaculatus

Biochem Biophys Res Commun. 1987 Dec 31;149(3):908-14. doi: 10.1016/0006-291x(87)90494-3.

Abstract

The octapeptide AKH-G, isolated from the cricket Gryllus bimaculatus, stimulates lipid mobilization in both the cricket itself and in migratory locusts. The structure of AKH-G has been assigned by fast atom bombardment mass spectrometry (FABMS) as pGlu-Val-Asn-Phe-Ser-Thr-Gly-Trp-NH2, and it is most closely related to AKH II-S from Schistocerca species, which has a Leu2 unit. Synthetic AKH-G, prepared by solid phase techniques, had the same bioactivity as the natural substance. FABMS measurements, including high-resolution and metastable studies, were made employing 400-900 pmole of sample.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Gryllidae / analysis*
  • Hemolymph / analysis
  • Insect Hormones / analysis*
  • Lipids / blood
  • Mass Spectrometry
  • Oligopeptides / analysis*
  • Orthoptera / analysis*
  • Pyrrolidonecarboxylic Acid / analogs & derivatives
  • Sequence Homology, Nucleic Acid
  • Species Specificity

Substances

  • Insect Hormones
  • Lipids
  • Oligopeptides
  • adipokinetic hormone
  • Pyrrolidonecarboxylic Acid