Isolation, identification, and synthesis of Mas-MG-MT I, a novel peptide from the larval midgut of Manduca sexta (Lepidoptera: Sphingidae).
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-NH2. 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.
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Laboratory of Agrozoology, Faculty of Agricultural and Applied Biological Sciences, University of Gent, Belgium.
Tirry
L
L
Bai
C
C
Devreese
B
B
Van Beeumen
J
J
Degheele
D
D
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005260:Female; D007422:Intestines / Q000737:chemistry; D007814:Larva; D018402:Manduca / Q000737:chemistry*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000302:isolation & purification*; D016339:Spectrometry, Mass, Fast Atom Bombardment
D000596:Amino Acids; D009842:Oligopeptides; C092644:alanyl-glutamyl-prolyl-tyrosyl-threoninamide