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Characterization of a diuretic peptide from Locusta migratoria
I Kay1, C H Wheeler, G M Coast
1Department of Biology, Birkbeck College, University of London, U.K.
Biological Chemistry Hoppe-Seyler
|October 1, 1991
Abstract:
A diuretic peptide Locusta-DP, identified by its ability to increase cyclic AMP production in locust Malpighian tubules in vitro, has been isolated and characterized from whole heads of Locusta migratoria. The purified peptide stimulates fluid secretion by Malpighian tubules maximally in vitro. The primary structure of Locusta-DP was established as a 46 residue amidated peptide: MGMGPSLSIVNPMDVLRQRLLLEIARRRLRDAEEQIKANKDFLQQI-NH2. Locusta-DP has 48% sequence identity with Acheta-DP and 49% identity with Manduca-DH, and provides further evidence for the presence of a family of diuretic peptides in insects.