Te. Taubmontemayor et al., ISOLATION AND CHARACTERIZATION OF MELANOPLUS-SANGUINIPES ADIPOKINETICHORMONE - A NEW MEMBER OF THE AKH RPCH FAMILY/, Biochemical and biophysical research communications, 239(3), 1997, pp. 763-768
A neuropeptide hormone isolated from corpora cardiaca of Melanoplus sa
nguinipes was purified by HPLC. The HPLC fractions were examined for a
dipokinetic activity with an in vivo bioassay. A single large UV absor
bent peak was active in the mobilization of lipid while the other HPLC
fractions showed no detectable activity. This large peak had a retent
ion time and amino acid composition identical to synthetic Lom-AHH-I w
hich was analyzed in a parallel manner. The primary sequence structure
, pGlu-Leu-Asn-Phe-Thr-Pro-Asn-Trp-Gly-Thr-NH2, was determined by auto
mated gas-phase Edman degradation. The peptide was deblocked prior to
sequencing using pyroglutamate aminopeptidase and the sequence was con
firmed with mass spectrometry. The C-terminus of the peptide was deter
mined to be blocked, as indicated by the lack of digestion with carbox
ypeptidase A. The knowledge of the primary sequence of Mes-AKH allows
the use of a commercially available synthetic peptide and its antibodi
es for use in future research with Melanoplus sanguinipes. (C) 1997 Ac
ademic Press.