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Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom
Citation
Torres, AM and Tsampazi, M and Kennett, EC and Belov, K and Geraghty, DP and Bansal, PS and Alewood, PF and Kuchel, PW, Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom, Amino Acids, 32, (1) pp. 63-68. ISSN 0939-4451 (2007) [Refereed Article]
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Copyright Statement
The original publication is available at www.springerlink.com
Official URL: http://www.springerlink.com
DOI: doi:10.1007/s00726-006-0346-6
Abstract
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 Details
Item Type: | Refereed Article |
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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 |
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