The corpora cardiaca (CC) of the pneumorid grasshopper species Bullacris discolor contain at least one substance that causes hyperlipaemia in the migratory locust. Isolation of neuropeptides belonging to the adipokinetic hormone (AKH) family was achieved by single-step reversed-phase high performance liquid chromatography (RP-HPLC) of CC extracts and monitoring tryptophan fluorescence. The material of the bladder grasshopper showed three distinct fluorescence peaks with adipokinetic activity in the migratory locust. The peptide sequences were identified by Edman degradation after the N-terminal pyroglutamate residue had been cleaved off enzymatically, and the exact peptide masses were determined by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Moreover, the assigned peptides were synthesised and natural and synthetic peptides were compared in their behaviour in RP-HPLC. B. discolor stores three AKH peptides in its CC: two of those are octapeptides, Schgr-AKH-II (pELNFSTGWamide) and Peram-CAH-II (pELTFTPNWamide), whereas the third peptide is a decapeptide, Phyle-CC (pELTFTPNWGSamide. The concentration of carbohydrates in the haemolymph of B. discolor is about 3 times higher than the lipid concentration. Upon injection with synthetic Schgr-AKH-II no adipokinetic or hypertrehalosaemic effect was measurable. A literature survey appears to indicate that an active role of these AKH peptides in substrate mobilisation is only overtly displayed in those caeliferan species that undertake well-defined flight periods.