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Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH sub 2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group
Authors:
Grimmelikhuijzen, C.J.P.
Jacob, E.
Graff, D.
Reinscheid, R.K.
Nothacker, H.P. (Univ. of Hamburg (West Germany))
Rinehart, K.L.
Staley, A.L. (Univ. of Illinois, Urbana (USA))
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| Abstract: Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Asn-NH 2, the authors have purified a peptide from acetic acid extracts of the sea anemone Anthopleura elegantissima.^By classical amino acid analyses, mass spectrometry, and 1H NMR spectroscopy, the structure of this peptide was determined as 3-phenyllactyl-Leu-Arg-Asn-NH 2.^By using reversed-phase HPLC and a chiral mobile phase, it was shown that the 3-phenyllactyl group had the L configuration.^Immunocytochemical staining with antiserum against Arg-Asn-NH 2 showed that L-3-phenyllactyl-Leu-Arg-Asn-NH 2 (Antho-RNamide) was localized in neutrons of sea anemones.^The L-3-phenyllactyl group has not been found earlier in neuropeptides of vertebrates or higher invertebrates.^They propose that this residue renders Antho-RNamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the peptide after neuronal release. |
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| Publication Date: |
01 Jul 1990
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| Resource Type: |
Journal Article
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| Resource Relation: |
Proceedings of the National Academy of Sciences of the United States of America ; Vol/Issue: 87:14
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| Country of Publication: |
United States
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| Language: |
English
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Keywords relating to this report: 
