The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity

C Schmutzler; D Diekhoff; C J Grimmelikhuijzen

The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity

C Schmutzler, D Diekhoff, C J Grimmelikhuijzen

Cell and Neurobiology

20 Citations (Scopus)

Abstract

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 (

Original language	English
Journal	Biochemical Journal
Volume	299 ( Pt 2)
Issue number	299
Pages (from-to)	431-436
Number of pages	6
ISSN	0264-6021
Publication status	Published - 15 Apr 1994

Keywords

Amino Acid Sequence
Animals
Base Sequence
Biological Evolution
Cnidaria
Endopeptidases
Gene Library
Insect Hormones
Molecular Sequence Data
Neuropeptides
Oligodeoxyribonucleotides
Protein Precursors
Protein Processing, Post-Translational
Protein Sorting Signals
Restriction Mapping
Sequence Homology, Amino Acid

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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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abstract = "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 (",

keywords = "Amino Acid Sequence, Animals, Base Sequence, Biological Evolution, Cnidaria, Endopeptidases, Gene Library, Insect Hormones, Molecular Sequence Data, Neuropeptides, Oligodeoxyribonucleotides, Protein Precursors, Protein Processing, Post-Translational, Protein Sorting Signals, Restriction Mapping, Sequence Homology, Amino Acid",

author = "C Schmutzler and D Diekhoff and Grimmelikhuijzen, {C J}",

year = "1994",

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language = "English",

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pages = "431--436",

journal = "Biochemical Journal",

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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

SN - 0264-6021

VL - 299 ( Pt 2)

SP - 431

EP - 436

JO - Biochemical Journal

JF - Biochemical Journal

IS - 299

ER -

The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity

Abstract

Keywords

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