Format

Send to

Choose Destination
See comment in PubMed Commons below
Amino Acids. 2007 Jan;32(1):63-8. Epub 2006 May 26.

Characterization and isolation of L-to-D-amino-acid-residue isomerase from platypus venom.

Author information

  • 1School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia.

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 degrees 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).

PMID:
16729187
DOI:
10.1007/s00726-006-0346-6
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center