The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity
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The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity. / Schmutzler, C; Diekhoff, D; Grimmelikhuijzen, C J.
In: Biochemical Journal, Vol. 299 ( Pt 2), No. 299, 15.04.1994, p. 431-436.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity
AU - Schmutzler, C
AU - Diekhoff, D
AU - Grimmelikhuijzen, C J
PY - 1994/4/15
Y1 - 1994/4/15
N2 - Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 (RFamide) occur throughout the Animal Kingdom and are abundant in evolutionarily 'old' nervous systems such as those of cnidarians. From the hydromedusa Polyorchis penicillatus we have previously isolated two neuropeptides, Pol-RFamide I (
AB - Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 (RFamide) occur throughout the Animal Kingdom and are abundant in evolutionarily 'old' nervous systems such as those of cnidarians. From the hydromedusa Polyorchis penicillatus we have previously isolated two neuropeptides, Pol-RFamide I (
KW - Amino Acid Sequence
KW - Animals
KW - Base Sequence
KW - Biological Evolution
KW - Cnidaria
KW - Endopeptidases
KW - Gene Library
KW - Insect Hormones
KW - Molecular Sequence Data
KW - Neuropeptides
KW - Oligodeoxyribonucleotides
KW - Protein Precursors
KW - Protein Processing, Post-Translational
KW - Protein Sorting Signals
KW - Restriction Mapping
KW - Sequence Homology, Amino Acid
M3 - Journal article
C2 - 7909659
VL - 299 ( Pt 2)
SP - 431
EP - 436
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 299
ER -
ID: 248899