Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

Harvard

Grimmelikhuijzen, CJ, Rinehart, KL, Jacob, E, Ebbesen, DG, Reinscheid, RK, Nothacker, HP & Staley, AL 1990, 'Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group', Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 14, pp. 5410-4.

APA

Grimmelikhuijzen, C. J., Rinehart, K. L., Jacob, E., Ebbesen, D. G., Reinscheid, R. K., Nothacker, H. P., & Staley, A. L. (1990). Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group. Proceedings of the National Academy of Sciences of the United States of America, 87(14), 5410-4.

Vancouver

Grimmelikhuijzen CJ, Rinehart KL, Jacob E, Ebbesen DG, Reinscheid RK, Nothacker HP et al. Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group. Proceedings of the National Academy of Sciences of the United States of America. 1990 Jul 1;87(14):5410-4.

Author

Grimmelikhuijzen, C J ; Rinehart, K L ; Jacob, E ; Ebbesen, Ditte Graff ; Reinscheid, R K ; Nothacker, H P ; Staley, A L. / Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group. In: Proceedings of the National Academy of Sciences of the United States of America. 1990 ; Vol. 87, No. 14. pp. 5410-4.

Bibtex

@article{820f0984b3be487a99d906836fbdc771,
title = "Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group",
abstract = "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.",
keywords = "Amino Acid Sequence, Animals, Antibody Specificity, Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Cnidaria, Mass Spectrometry, Molecular Sequence Data, Neuropeptides, Oligopeptides, Radioimmunoassay, Sea Anemones, Sequence Homology, Nucleic Acid, Species Specificity",
author = "Grimmelikhuijzen, {C J} and Rinehart, {K L} and E Jacob and Ebbesen, {Ditte Graff} and Reinscheid, {R K} and Nothacker, {H P} and Staley, {A L}",
year = "1990",
month = jul,
day = "1",
language = "English",
volume = "87",
pages = "5410--4",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "14",

}

RIS

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