Isolation and characterization of Melanoplus sanguinipes adipokinetic hormone: a new member of the AKH/RPCH family

Biochemical and Biophysical Research Communications
Tina E Taub-MontemayorMary Ann Rankin


A neuropeptide hormone isolated from corpora cardiaca of Melanoplus sanguinipes was purified by HPLC. The HPLC fractions were examined for adipokinetic activity with an in vivo bioassay. A single large UV absorbent peak was active in the mobilization of lipid while the other HPLC fractions showed no detectable activity. This large peak had a retention time and amino acid composition identical to synthetic Lom-AKH-I which was analyzed in a parallel manner. The primary sequence structure, pGlu-Leu-Asn-Phe-Thr-Pro-Asn-Trp-Gly-Thr-NH2, was determined by automated gas-phase Edman degradation. The peptide was deblocked prior to sequencing using pyroglutamate aminopeptidase and the sequence was confirmed with mass spectrometry. The C-terminus of the peptide was determined to be blocked, as indicated by the lack of digestion with carboxypeptidase A. The knowledge of the primary sequence of Mes-AKH allows the use of a commercially available synthetic peptide and its antibodies for use in future research with Melanoplus sanguinipes.


Dec 24, 2003·Archives of Insect Biochemistry and Physiology·Kyung Jin MinMary Ann Rankin
Jun 7, 2005·Mass Spectrometry Reviews·Amanda B HummonJonathan V Sweedler

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