ISOLATION OF LEU-PRO-PRO-GLY-PRO-LEU-PRO-ARGPRO-NH2 (ANTHO-RPAMIDE), AN N-TERMINALLY PROTECTED, BIOLOGICALLY-ACTIVE NEUROPEPTIDE FROM SEA-ANEMONES

被引：25

作者：

CARSTENSEN, K

RINEHART, KL

MCFARLANE, ID

GRIMMELIKHUIJZEN, CJP

机构：

[1] UNIV HAMBURG,CTR MOLEC NEUROBIOL,MARTINISTR 52,W-2000 HAMBURG 20,GERMANY

[2] UNIV ILLINOIS,SCH CHEM SCI,URBANA,IL 61801

[3] UNIV HULL,DEPT APPL BIOL,HULL HU6 7RX,N HUMBERSIDE,ENGLAND

来源：

PEPTIDES | 1992年 / 13卷 / 05期

关键词：

NEUROHORMONE; NEUROTRANSMITTER; NEUROPEPTIDE PROTECTING SEQUENCE; PEPTIDE STRUCTURE; RADIOIMMUNOASSAY; MASS SPECTROMETRY; COELENTERATE; BRADYKININ; ANGIOTENSIN-I CONVERTING ENZYME;

D O I：

10.1016/0196-9781(92)90040-A

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Using a radioimmunoassay against the C-terminal sequence Arg-Pro-NH2 (RPamide), we have isolated the peptide Leu-Pro-Pro-Gly-Pro-Leu-Pro-Arg-Pro-NH2 (Antho-RPamide) from an extract of the sea anemone Anthopleura elegantissima. Antho-RPamide is located in neurons of sea anemones. Application of low concentrations of Antho-RPamide to tentacle preparations of sea anemones strongly increased the frequency and duration of spontaneous contractions, suggesting that this peptide is involved in neurotransmission. Antho-RPamide has a free N-terminus, yet its X-Pro-Pro sequence makes it relatively resistant to degradation by nonspecific aminopeptidases. Thus, we have discovered another strategy by which sea anemones protect the N-termini of their bioactive neuropeptides.

引用

页码：851 / 857

页数：7

共 22 条

[1] MICRO-SEQUENCE ANALYSIS OF PEPTIDES AND PROTEINS USING 4-NN-DIMETHYLAMINOAZOBENZENE 4'-ISOTHIOCYANATE-PHENYLISOTHIOCYANATE DOUBLE COUPLING METHOD [J].