Abstract
The nervous system and gut of Aplysia and other gastropod molluscs contain several classes of cardioactive peptides1. In addition to their excitatory action on the heart, these peptides stimulate contractile activity in the gut1, and modulate neurally induced contractions of somatic muscles2. This report describes the purification and sequence determination by a combination of microprotein chemistry and fast atom bombardment mass spectrometry FAB–MS3,4 of one of these peptides. The sequenced peptide is a member of the small class of cardioactive peptides and was termed SCPB. A peptide with identical properties to SCPB has been found in several identified central neurones which innervate the gut5. Here we report the structure of SCPB as a C-terminally blocked peptide H-Met-Asn-Tyr-Leu-Ala-Phe-Pro-Arg-Met-NH2 Native and synthetic SCPB have identical actions on molluscan muscle preparations with thresholds at around 10−10 M.
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Morris, H., Panico, M., Karplus, A. et al. Elucidation by FAB–MS of the structure of a new cardioactive peptide from Aplysia. Nature 300, 643–645 (1982). https://doi.org/10.1038/300643a0
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DOI: https://doi.org/10.1038/300643a0
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