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Platypus venom contains an isomerase that reversibly interconverts the second amino-acid residue in some peptides between the L-form and the D-form. The enzyme acts on the natriuretic peptides OvCNPa and OvCNPb, and on the defensin-like peptides DLP-2 and DLP-4, but it does not act on DLP-1. While the isomerization of DLP-2 to DLP-4 is inhibited by the amino-peptidase inhibitor amastatin, it is not affected by the leucine amino-peptidase inhibitor bestatin. The enzyme, that is only present in minute quantities in an extract of the venom gland, is thermally stable up to 55 °C, and it was found by anion-exchange chromatography to be acidic. Isolation of the isomerase was carried out by combined ion-exchange chromatography and reverse-phase high performance liquid chromatography (HPLC).

Item Type:	Refereed Article
Keywords:	DLP – Peptide isomerase – Platypus venom peptides
Research Division:	Biomedical and Clinical Sciences
Research Group:	Medical biochemistry and metabolomics
Research Field:	Medical biochemistry - proteins and peptides (incl. medical proteomics)
Objective Division:	Environmental Management
Objective Group:	Terrestrial systems and management
Objective Field:	Terrestrial biodiversity
UTAS Author:	Geraghty, DP (Professor Dominic Geraghty)
ID Code:	39387
Year Published:	2007
Web of Science® Times Cited:	30
Deposited By:	Health Sciences A
Deposited On:	2007-08-01
Last Modified:	2012-04-20
Downloads:	0