Primary sequence analysis by fast atom bombardment mass spectrometry of a peptide with adipokinetic activity from the corpora cardiaca of the cricket Gryllus bimaculatus.
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.
Gäde
G
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Institut für Zoologie IV, Universität Düsseldorf, F.R.G.
Rinehart
K L
KL
D000595:Amino Acid Sequence; D000818:Animals; D006135:Gryllidae / Q000032:analysis*; D006458:Hemolymph / Q000032:analysis; D007301:Insect Hormones / Q000032:analysis*; D008055:Lipids / Q000097:blood; D013058:Mass Spectrometry; D009842:Oligopeptides / Q000032:analysis*; D009987:Orthoptera / Q000032:analysis*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D007301:Insect Hormones; D008055:Lipids; D009842:Oligopeptides; C044833:adipokinetic hormone; D011761:Pyrrolidonecarboxylic Acid