Lepidopteran peptides of the allatostatin superfamily.
Peptides of the allatostatin superfamily with the C-terminal amino acid sequence -YXFGL-NH2 have been isolated and identified from the lepidopterans, the codling moth, Cydia pomonella (Tortricidae) and the bollworm, Helicoverpa armigera (Noctuidae). The peptides, designated cydiastatins and helicostatins respectively, were monitored during purification with radioimmunoassays based on the callatostatins of the blowfly Calliphora vomitoria. The eight peptides from each of the two species appear to form an homologous series with four identical and three that differ by a single amino acid. This study demonstrates the ubiquitous nature of this family of peptides in insects.
Duve
H
H
School of Biological Sciences, Queen Mary & Westfield College, University of London, UK.
Johnsen
A H
AH
Maestro
J L
JL
Scott
A G
AG
Winstanley
D
D
Davey
M
M
East
P D
PD
Thorpe
A
A
D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D009036:Moths / Q000737:chemistry*; D005810:Multigene Family; D009479:Neuropeptides / Q000235:genetics* / Q000302:isolation & purification*; D011863:Radioimmunoassay
D009479:Neuropeptides; C076523:allatostatin