Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones
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Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones. / Grimmelikhuijzen, C J; Ebbesen, Ditte Graff.
I: Proceedings of the National Academy of Sciences of the United States of America, Bind 83, Nr. 24, 01.12.1986, s. 9817-21.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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