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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 NH2-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.
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Wagner et al. (1997) studied this question.
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