| Literature DB >> 2432065 |
M S Leisola, B Kozulic, F Meussdoerffer, A Fiechter.
Abstract
The extracellular peroxidases of Phanerochaete chrysosporium were separated into 21 proteins by analytical isoelectric focusing. Fifteen of these enzymes oxidized veratryl alcohol (lignin peroxidases) in the presence of H2O2. Six enzymes were Mn(II)-dependent peroxidases. The Mn(II)-dependent enzymes appeared and reached their maximal activity earlier than the lignin peroxidases in the cultures. Peptide mapping, amino acid analysis, and reaction against specific antibodies showed that all the Mn(II)-dependent peroxidases were probably products of one gene. A great degree of homology was also present among the various lignin peroxidases.Entities:
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Year: 1987 PMID： 2432065
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157