GNFFRFAMIDE - A NOVEL FMRFAMIDE-IMMUNOREACTIVE PEPTIDE ISOLATED FROM THE SHEEP TAPEWORM, MONIEZIA-EXPANSA

被引：68

作者：

MAULE, A ^{[1
]}

SHAW, C ^{[1
]}

HALTON, D ^{[1
]}

THIM, L ^{[1
]}

机构：

[1] NOVO NORDISK AS,BAGSVAERD,DENMARK

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 193卷 / 03期

关键词：

D O I：

10.1006/bbrc.1993.1732

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：

The widespread distribution of FMRFamide-immunoreactivity in platyhelminth nervous systems has been demonstrated immunocytochemically. Here we report the isolation and primary structure of the first platyhelminth FMRFamide-related peptide (FaRP) from the tapeworm, Moniezia expansa. The peptide was found to have a molecular mass of 785 Da and a primary structure of Gly-Asn-Phe-Arg-Phe-NH2 (GNFFRFamide). Acid alcohol extracts of this platyhelminth contained only this single FaRP which had a phenylalanyl (F) residue in the variable position 3 from the C-terminal occupied by either methionyl (M), leucyl (L) or isoleucyl (I) residues in most other FaRPs. © 1993 Academic Press, Inc.

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页码：1054 / 1060

页数：7

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