caa a22 4500 463185293 CHVBK 20180406164851.0 cr unu---uuuuu 170326e20070101xx s 000 0 eng 10.1007/s00726-006-0346-6 doi (NATIONALLICENCE)springer-10.1007/s00726-006-0346-6 Characterization and isolation of L -to- D -amino-acid-residue isomerase from platypus venom [Elektronische Daten] [A. M. Torres, M. Tsampazi, E. C. Kennett, K. Belov, D. P. Geraghty, P. S. Bansal, P. F. Alewood, P. W. Kuchel] Summary.: 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). Springer-Verlag, 2006 Keywords: DLP - Peptide isomerase - Platypus venom peptides nationallicence Torres A. M. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut Tsampazi M. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut Kennett E. C. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut Belov K. Faculty of Veterinary Science, University of Sydney, Camden, Australia aut Geraghty D. P. School of Human Life Sciences, University of Tasmania, Launceston, Australia aut Bansal P. S. Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia aut Alewood P. F. Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia aut Kuchel P. W. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut Amino Acids Springer-Verlag 32/1(2007-01-01), 63-68 0939-4451 32:1<63 2007 32 726 https://doi.org/10.1007/s00726-006-0346-6 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0346-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Torres A. M. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut NATIONALLICENCE 700 1- Tsampazi M. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut NATIONALLICENCE 700 1- Kennett E. C. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut NATIONALLICENCE 700 1- Belov K. Faculty of Veterinary Science, University of Sydney, Camden, Australia aut NATIONALLICENCE 700 1- Geraghty D. P. School of Human Life Sciences, University of Tasmania, Launceston, Australia aut NATIONALLICENCE 700 1- Bansal P. S. Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia aut NATIONALLICENCE 700 1- Alewood P. F. Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia aut NATIONALLICENCE 700 1- Kuchel P. W. School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 32/1(2007-01-01), 63-68 0939-4451 32:1<63 2007 32 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer