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PMID: 3426616 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Biochemical and biophysical research communications ·Vol. 149 ·No. 3 ·1987-12-31 ·Pages 908-14

Gäde G, Rinehart KL

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.

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
Chemicals
Insect Hormones Lipids Oligopeptides adipokinetic hormone Pyrrolidonecarboxylic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gäde G
Institut für Zoologie IV, Universität Düsseldorf, F.R.G.
Rinehart K L
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1987-12-31
Pages
908-14
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NIGMS NIH HHS · GM 27029 · United States
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