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Identification and characterization of an ecdysiotropic peptide from brain extracts of the gypsy moth, Lymantria dispar
Author(s) -
Wagner R.M.,
Loeb M.J.,
Kochansky J.P.,
Gelman D.B.,
Lusby W.R.,
Bell R.A.
Publication year - 1997
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1997)34:2<175::aid-arch4>3.0.co;2-w
Subject(s) - lymantria dispar , gypsy moth , ecdysteroid , biology , peptide , dispar , lepidoptera genitalia , pupa , larva , insect , peptide sequence , biochemistry , microbiology and biotechnology , botany , genetics , gene , entamoeba histolytica
A peptide ( Lymantria TE) was isolated from brains of the gypsy moth, Lymantria dispar , which stimulates synthesis of ecdysteroid in the testes of larval and pupal insects. This ecdysiotropic peptide was purified and its structure determined to be NH 2 ‐IIe‐Ser‐Asp‐Phe‐Asp‐Glu‐Tyr‐Glu‐Pro‐Leu‐Asn‐Asp‐Ala‐Asp‐Asn‐Asn‐Glu‐Val‐Leu‐Asp‐Phe‐OH using protein sequence analysis and electrospray mass spectrometry. The peptide was biphasic in activity, with maximal activity in the pupal testes at 10 −13 M and 10 −9 M, with a minimum at 10 −10 M, and with maxima at 10 −15 M and 10 −10 M and minimum at 10 −13 M for larval testes. Arch. Insect Biochem. Physiol. 34:175–189, 1997. © 1997 Wiley‐Liss, Inc. This article is a US Government work and, as such, is in the public domain in the United States of America.