Neuropeptide F: primary structure from the tubellarian, Artioposthia triangulata.

Publication Type:Journal Article
Year of Publication:1992
Authors:W. J. Curry, Shaw, C., Johnston, C. F., Thim, L., Buchanan, K. D.
Journal:Comp Biochem Physiol C
Volume:101
Issue:2
Pagination:269-74
Date Published:1992 Feb
ISSN:0742-8413
Keywords:Amino Acid Sequence, Animals, Helminth Proteins, Immunohistochemistry, Mass Spectrometry, Molecular Sequence Data, Molecular Weight, Neuropeptide Y, Neuropeptides, Pancreatic Polypeptide, Platyhelminths, Sequence Homology, Nucleic Acid
Abstract:

1. A neuropeptide exhibiting vertebrate pancreatic polypeptide immunoreactivity has been isolated and sequenced from extracts of the terrestrial turbellarian, Artioposthia triangulata. 2. This neuropeptide, designated neuropeptide F, consists of 36 amino acid residues terminating in a phenylalaninamide. 3. The full primary structure was established as: KVVHLRPRSSFSSEDEYQIYLRNVSKYIQLYGRPRF.NH2. The molecular mass, deduced from this sequence, was 4433 Da. 4. This neuropeptide exhibits C-terminal homology with neuropeptide F (Moniezia expansa) and with the vertebrate neuropeptide Y/pancreatic polypeptide superfamily of which it may represent a phylogenetic precursor.

Alternate Journal:Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol.
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