| Title: | "Isolation, identification and synthesis of locustamyotropin (Lom-MT), a novel biologically active insect peptide" |
| Author(s): | Schoofs L; Holman GM; Hayes TK; Tips A; Nachman RJ; Vandesande F; De Loof A; |
| Address: | "Zoological Institute, Katholieke Universiteit Leuven, Belgium" |
| DOI: | 10.1016/0196-9781(90)90038-7 |
| ISSN/ISBN: | 0196-9781 (Print) 0196-9781 (Linking) |
| Abstract: | "A peptide that stimulates the spontaneous contractions of the hindgut of Leucophaea maderae has been purified from extracts of brain-corpora cardiaca/corpora allata-subesophageal ganglion complexes of 9000 adult Locusta migratoria and was designated locustamyotropin or Lom-MT. The primary structure of this 12 residue peptide has been determined Gly-Ala-Val-Pro-Ala-Ala-Gln-Phe-Ser-Pro-Arg-Leu-NH2. The C-terminal sequence (Phe-Ser-Pro-Arg-Leu-NH2) is identical to the C-terminal pentapeptide of the pheromone biosynthesis activating neuropeptide, recently isolated from Heliothis zea, and is also similar to the C-terminal of leucopyrokinin of Leucophaea. Synthetic Lom-MT showed biological as well as chemical characteristics, indistinguishable from those of native Lom-MT. In locust preparations, Lom-MT provoked an increase in frequency, amplitude and tonus of contractions of the oviduct, but was inactive in the same conditions on the locust hindgut preparation" |
| Keywords: | "Amino Acid Sequence Aminopeptidases Animals Biological Assay CD13 Antigens Chromatography, High Pressure Liquid Grasshoppers/*analysis Molecular Sequence Data Neuropeptides/analysis/chemical synthesis/*isolation & purification Sequence Homology, Nucleic A;" |
| Notes: | "MedlineSchoofs, L Holman, G M Hayes, T K Tips, A Nachman, R J Vandesande, F De Loof, A eng R0INS20137/NS/NINDS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1990/05/01 Peptides. 1990 May-Jun; 11(3):427-33. doi: 10.1016/0196-9781(90)90038-7" |
