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Isolation, identification, and synthesis of Mas‐MG‐MT I, a novel peptide from the larval midgut of Manduca sexta (lepidoptera: Sphingidae)
Author(s) -
Yi S.X.,
Tirry L.,
Bai C.,
Devreese B.,
van Beeumen J.,
Degheele D.
Publication year - 1995
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/arch.940280206
Subject(s) - manduca sexta , sphingidae , biology , midgut , manduca , peptide sequence , peptide , biochemistry , insect , oviduct , lepidoptera genitalia , microbiology and biotechnology , larva , botany , endocrinology , gene
A five‐residue myotropic peptide, Manduca sexta midgut myotropin I (Mas‐MG‐MT I), was isolated from an extract of 800 midguts of fifth instar larvae of the tobacco hornworm, Manduca sexta . It was purified by reverse phase and normal phase HPLC. Myotropic activity was screened by a heterologous Locusta migratoria oviduct bioassay. Sequence analysis, amino acid composition analysis, and comparison of candidate synthetic peptides in the amide and acid form revealed the following primary structure: Ala‐Glu‐Pro‐Tyr‐Thr‐NH 2 . This is the first fully identified peptide isolated directly from the midgut of an insect species. Few significant sequence homologies with known vertebrate and invertebrate peptides have been found. © 1995 Wiley‐Liss, Inc.