Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones

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Standard

Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones. / Grimmelikhuijzen, C J; Ebbesen, Ditte Graff.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, No. 24, 01.12.1986, p. 9817-21.

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

Harvard

Grimmelikhuijzen, CJ & Ebbesen, DG 1986, 'Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones', Proceedings of the National Academy of Sciences of the United States of America, vol. 83, no. 24, pp. 9817-21.

APA

Grimmelikhuijzen, C. J., & Ebbesen, D. G. (1986). Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones. Proceedings of the National Academy of Sciences of the United States of America, 83(24), 9817-21.

Vancouver

Grimmelikhuijzen CJ, Ebbesen DG. Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones. Proceedings of the National Academy of Sciences of the United States of America. 1986 Dec 1;83(24):9817-21.

Author

Grimmelikhuijzen, C J ; Ebbesen, Ditte Graff. / Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones. In: Proceedings of the National Academy of Sciences of the United States of America. 1986 ; Vol. 83, No. 24. pp. 9817-21.

Bibtex

@article{4a2d9aa0b92c4a1fa4f39bffc1d4f974,
title = "Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones",
abstract = "A radioimmunoassay has been developed for peptides containing the carboxyl-terminal sequence Arg-Phe-NH2 (RFamide). Using this radioimmunoassay and applying cation-exchange chromatography and HPLC, we have isolated an RFamide peptide from acetic acid extracts of the sea anemone Anthopleura elegantissima. Three different methods established that the structure of the Anthopleura RFamide peptide (Antho-RFamide) is pyroGlu-Gly-Arg-Phe-NH2. Comparison of synthetic and natural Antho-RFamide and their enzymatic breakdown products on six different HPLC columns confirmed the structure of the sea anemone peptide. Using synthetic Antho-RFamide as a standard in our radioimmunoassay, we measured high concentrations (3.2 nmol/g wet weight) of this peptide in extracts of Anthopleura. It is proposed that Antho-RFamide is a transmitter at neuromuscular synapses in sea anemones.",
keywords = "Amino Acid Sequence, Animals, Chromatography, High Pressure Liquid, Cnidaria, Neuropeptides, Oligopeptides, Radioimmunoassay, Sea Anemones",
author = "Grimmelikhuijzen, {C J} and Ebbesen, {Ditte Graff}",
year = "1986",
month = dec,
day = "1",
language = "English",
volume = "83",
pages = "9817--21",
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 = "24",

}

RIS

TY - JOUR

T1 - Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones

AU - Grimmelikhuijzen, C J

AU - Ebbesen, Ditte Graff

PY - 1986/12/1

Y1 - 1986/12/1

N2 - A radioimmunoassay has been developed for peptides containing the carboxyl-terminal sequence Arg-Phe-NH2 (RFamide). Using this radioimmunoassay and applying cation-exchange chromatography and HPLC, we have isolated an RFamide peptide from acetic acid extracts of the sea anemone Anthopleura elegantissima. Three different methods established that the structure of the Anthopleura RFamide peptide (Antho-RFamide) is pyroGlu-Gly-Arg-Phe-NH2. Comparison of synthetic and natural Antho-RFamide and their enzymatic breakdown products on six different HPLC columns confirmed the structure of the sea anemone peptide. Using synthetic Antho-RFamide as a standard in our radioimmunoassay, we measured high concentrations (3.2 nmol/g wet weight) of this peptide in extracts of Anthopleura. It is proposed that Antho-RFamide is a transmitter at neuromuscular synapses in sea anemones.

AB - A radioimmunoassay has been developed for peptides containing the carboxyl-terminal sequence Arg-Phe-NH2 (RFamide). Using this radioimmunoassay and applying cation-exchange chromatography and HPLC, we have isolated an RFamide peptide from acetic acid extracts of the sea anemone Anthopleura elegantissima. Three different methods established that the structure of the Anthopleura RFamide peptide (Antho-RFamide) is pyroGlu-Gly-Arg-Phe-NH2. Comparison of synthetic and natural Antho-RFamide and their enzymatic breakdown products on six different HPLC columns confirmed the structure of the sea anemone peptide. Using synthetic Antho-RFamide as a standard in our radioimmunoassay, we measured high concentrations (3.2 nmol/g wet weight) of this peptide in extracts of Anthopleura. It is proposed that Antho-RFamide is a transmitter at neuromuscular synapses in sea anemones.

KW - Amino Acid Sequence

KW - Animals

KW - Chromatography, High Pressure Liquid

KW - Cnidaria

KW - Neuropeptides

KW - Oligopeptides

KW - Radioimmunoassay

KW - Sea Anemones

M3 - Journal article

C2 - 2879288

VL - 83

SP - 9817

EP - 9821

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 - 24

ER -

ID: 33514576