ISOLATION OF L-3-PHENYLLACTYL-LEU-ARG-ASN-NH2 (ANTHO-RNAMIDE), A SEA-ANEMONE NEUROPEPTIDE CONTAINING AN UNUSUAL AMINO-TERMINAL BLOCKING GROUP

被引：29

作者：

GRIMMELIKHUIJZEN, CJP ^{[1
]}

RINEHART, KL ^{[1
]}

JACOB, E ^{[1
]}

GRAFF, D ^{[1
]}

REINSCHEID, RK ^{[1
]}

NOTHACKER, HP ^{[1
]}

STALEY, AL ^{[1
]}

机构：

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

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 14期

关键词：

Coelenterate; Mass spectrometry; Neurotransmitter; Peptide hormone; Posttranslational modification;

D O I：

10.1073/pnas.87.14.5410

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Asn-NH2, we have purified a peptide from acetic acid extracts of the sea anemone Anthopleura elegantissima. By classical amino acid analyses, mass spectrometry, and 1H NMR spectroscopy, the structure of this peptide was determined as 3-phenyllactyl-Leu-Arg-Asn-NH2. By using reversed-phase HPLC and a chiral mobile phase, it was shown that the 3-phenyllactyl group had the L configuration. Immunocytochemical staining with antiserum against Arg-Asn-NH2 showed that L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide) was localized in neurons of sea anemones. The L-3-phenyllactyl group has not been found earlier in neuropeptides of vertebrates or higher invertebrates. We propose that this residue renders Antho-RNamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the peptide after neuronal release.

引用

页码：5410 / 5414

页数：5

共 32 条

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