Novel natriuretic peptides from the venom of the inland taipan (Oxyuranus microlepidotus): isolation, chemical and biological characterisation

Fry, B. G., Wickramaratana, J., Lemme, S., Beuve, A., Garbers, D., Hodgson, W. C. and Alewood, P. F. (2005) Novel natriuretic peptides from the venom of the inland taipan (Oxyuranus microlepidotus): isolation, chemical and biological characterisation. Biochemical and Biophysical Research Communications, 327 4: 1011-1015. doi:10.1016/j.bbrc.2004.11.171


Author Fry, B. G.
Wickramaratana, J.
Lemme, S.
Beuve, A.
Garbers, D.
Hodgson, W. C.
Alewood, P. F.
Title Novel natriuretic peptides from the venom of the inland taipan (Oxyuranus microlepidotus): isolation, chemical and biological characterisation
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 0006-291X
Publication date 2005
Sub-type Article (original research)
DOI 10.1016/j.bbrc.2004.11.171
Volume 327
Issue 4
Start page 1011
End page 1015
Total pages 5
Place of publication New York
Publisher Elsevier
Collection year 2005
Language eng
Subject C1
250302 Biological and Medical Chemistry
780105 Biological sciences
Abstract Three natriuretic-like peptides (TNP-a, TNP-b, and TNP-c) were isolated from the venom of Oxyuranus microlepidotus (inland taipan) and were also present in the venoms of Oxyuranus scutellatus canni (New Guinea taipan) and Oxyuranus scutellatus scutellatus (coastal taipan). They were isolated by HPLC, characterised by mass spectrometry and Edman analysis, and consist of 35-39 amino acid residues. These molecules differ from ANP/BNP through replacement of invariant residues within the 17-membered ring structure and by inclusion of proline residues in the C-terminal tail. TNP-c was equipotent to ANP in specific GC-A assays or aortic ring assays whereas TNP-a and TNP-b were either inactive (GC-A over-expressing cells and endothelium-denuded aortic rings) or weakly active (endothelium-in tact aortic rings). TNP-a and TNP-b were also unable to competitively inhibit the binding of TNP-c in endothelium-denuded aortae (GC-A) or endothelium-in tact aortae (NPR-C). Thus, these naturally occurring isoforms provide a new platform for further investigation of structure-function relationships of natriuretic peptides. (C) 2004 Elsevier Inc. All rights reserved.
Keyword Biophysics
Natriuretic Peptide
Mass Spectrometry
Venom
Guanylyl Cyclase
Oxyuranus Microlepidotus
Platypus Ornithorhynchus-anatinus
Snake-venom
A Receptor
Family
Forms
Biochemistry & Molecular Biology
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 07:03:04 EST