l-to-d-peptide isomerase in male echidna venom1
Jennifer M. S. Koh A , Leesa Haynes B , Katherine Belov C and Philip W. Kuchel A D
+ Author Affiliations
- Author Affiliations
A School of Molecular Bioscience, Building G08, University of Sydney, Sydney, NSW 2006, Australia.
B Healesville Sanctuary, Badger Creek Road, Healesville, Vic. 3777, Australia.
C Faculty of Veterinary Science, University of Sydney, Sydney, NSW 2006, Australia.
D Corresponding author. Email: philip.kuchel@sydney.edu.au.
Australian Journal of Zoology 58(5) 284-288 https://doi.org/10.1071/ZO10045
Submitted: 21 June 2010 Accepted: 28 October 2010 Published: 8 December 2010
Abstract
The monotremes (the echidnas and the platypus) display both mammalian and reptilian features. Male monotremes have a bilateral crural gland that is connected via a duct to a spur on each hind limb. Male echidnas appear not to use their spurs as weapons in aggressive acts, but the crural system may have a role in reproductive behaviour because it appears only to be active during the breeding season. The secretions produced by the echidna’s crural gland have not hitherto been biochemically or pharmacologically characterised. We used reverse-phase high-performance liquid chromatography (RP-HPLC) to separate the components of echidna venom and compared the chromatograms with those from platypus venom. The echidna venom appears to contain fewer proteins and peptides than platypus venom; however, it appears to have defensin-like peptides that behave similarly on RP-HPLC to those in platypus venom. Like platypus venom, echidna venom has peptidyl aminoacyl l/d-peptide isomerase activity. An RP-HPLC-based assay showed that the second amino acid residue, of a probe synthetic hexapeptide, was converted into the d-form, when incubated with echidna venom.
Additional keywords: platypus, d-amino acid.
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