Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group
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Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group. / Grimmelikhuijzen, C J; Rinehart, K L; Jacob, E; Ebbesen, Ditte Graff; Reinscheid, R K; Nothacker, H P; Staley, A L.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 87, No. 14, 01.07.1990, p. 5410-4.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group
AU - Grimmelikhuijzen, C J
AU - Rinehart, K L
AU - Jacob, E
AU - Ebbesen, Ditte Graff
AU - Reinscheid, R K
AU - Nothacker, H P
AU - Staley, A L
PY - 1990/7/1
Y1 - 1990/7/1
N2 - Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Asn-NH2, we 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-NH2. 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-NH2 showed that L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide) was localized in neurons of sea anemones. The L-3-phenyllactyl group has not been found earlier in neuropeptides of vertebrates or higher invertebrates. We propose that this residue renders Antho-RNamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the peptide after neuronal release.
AB - Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Asn-NH2, we 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-NH2. 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-NH2 showed that L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide) was localized in neurons of sea anemones. The L-3-phenyllactyl group has not been found earlier in neuropeptides of vertebrates or higher invertebrates. We propose that this residue renders Antho-RNamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the peptide after neuronal release.
KW - Amino Acid Sequence
KW - Animals
KW - Antibody Specificity
KW - Chromatography, High Pressure Liquid
KW - Chromatography, Ion Exchange
KW - Cnidaria
KW - Mass Spectrometry
KW - Molecular Sequence Data
KW - Neuropeptides
KW - Oligopeptides
KW - Radioimmunoassay
KW - Sea Anemones
KW - Sequence Homology, Nucleic Acid
KW - Species Specificity
M3 - Journal article
C2 - 1973541
VL - 87
SP - 5410
EP - 5414
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 14
ER -
ID: 33514272