Structure, localization, and action of buccalin B: a bioactive peptide from Aplysia.
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.
Vilim
F S
FS
Center for Neurobiology and Behavior, New York State Psychiatric Institute, Columbia University, NY 10032.
Cropper
E C
EC
Rosen
S C
SC
Tenenbaum
R
R
Kupfermann
I
I
Weiss
K R
KR
D000595:Amino Acid Sequence; D000818:Animals; D001048:Aplysia / Q000737:chemistry*; D001143:Arousal / Q000502:physiology; D005247:Feeding Behavior / Q000502:physiology; D007553:Isotope Labeling; D008564:Membrane Potentials; D008969:Molecular Sequence Data; D009046:Motor Neurons / Q000737:chemistry* / Q000187:drug effects; D009119:Muscle Contraction / Q000187:drug effects; D018485:Muscle Fibers, Skeletal / Q000187:drug effects; D009479:Neuropeptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid
D009479:Neuropeptides; C090829:buccalin B; C058692:buccalin