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Characterization of wood decay enzymes by MALDI-MS for post-translational modification and gene identification.Author(s): Theodorus H. de Koker; Philip J. Kersten
Source: Thirty-third annual meeting of the International Research Group on Wood Preservation, 2002 May 12-17, Cardiff, South Wales, UK. Stockholm, Sweden : IRG Secretariat, 2002. IRG/WP ; 02-10442: 8 pages.
Publication Series: Miscellaneous Publication
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DescriptionThe recent sequencing of the Phanerochaete chrysosporium genome presents many opportunities, including the possibility of rapidly correlating specific wood decay proteins of the fungus with the corresponding gene sequences. Here we compare mass fragments of trypsin digests, determined by MALDI-MS (Matrix Assisted Laser Desorption Ionization-Mass Spectrometry), with predicted mass fragments derived from genome sequence. Glyoxal oxidase of P. chrysosporium is used for proof of concept because its genomic organization is known. Glyoxal oxidase was also chosen because it is a glycoprotein, as are many other fungal proteins, and post-translational sites are predicted by MALDI-MS.
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Citationde Koker, Theodorus H.; Kersten, Philip J. 2002. Characterization of wood decay enzymes by MALDI-MS for post-translational modification and gene identification. Thirty-third annual meeting of the International Research Group on Wood Preservation, 2002 May 12-17, Cardiff, South Wales, UK. Stockholm, Sweden : IRG Secretariat, 2002. IRG/WP ; 02-10442: 8 pages.
KeywordsPhanerochaete chrysosporium, MALDI-MS, glyoxal oxidase.
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