Structure, localization, and action of buccalin B: a bioactive peptide from Aplysia

Peptides. 1994;15(6):959-69. doi: 10.1016/0196-9781(94)90058-2.

Abstract

The cholinergic motor neurons for the accessory radula closer (ARC) contain several neuropeptides that affect muscle contractions. In the present study, we have purified and sequenced a sixth ARC neuropeptide, using a combination of high pressure liquid chromatography and bioassays. This neuropeptide, Gly-Leu-Asp-Arg-Tyr-Gly-Phe-Val-Gly-Gly-Leu-amide, has been named buccalin B (BUCb) because it is significantly homologous to the previously characterized neuropeptide buccalin A. BUCb was found to be two-three times more potent than buccalin A in depressing motor neuron induced contractions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aplysia / chemistry*
  • Arousal / physiology
  • Feeding Behavior / physiology
  • Isotope Labeling
  • Membrane Potentials
  • Molecular Sequence Data
  • Motor Neurons / chemistry*
  • Motor Neurons / drug effects
  • Muscle Contraction / drug effects
  • Muscle Fibers, Skeletal / drug effects
  • Neuropeptides / chemistry*
  • Neuropeptides / isolation & purification
  • Neuropeptides / pharmacology
  • Sequence Homology, Amino Acid

Substances

  • Neuropeptides
  • buccalin B
  • buccalin