Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system

Elizabeth A. Pease, Steven D. Aust, Ming Tien

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.

Original languageEnglish (US)
Pages (from-to)897-903
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume179
Issue number2
DOIs
StatePublished - Sep 16 1991

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manganese peroxidase
Phanerochaete
Baculoviridae
Isoenzymes
Enzymes
Phenolsulfonphthalein
Guaiacol
Sf9 Cells
Post Translational Protein Processing
Polyacrylamide Gel Electrophoresis
Complementary DNA
Molecular Weight
Molecular weight
Antibodies
Substrates

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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abstract = "The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.",
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Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system. / Pease, Elizabeth A.; Aust, Steven D.; Tien, Ming.

In: Biochemical and Biophysical Research Communications, Vol. 179, No. 2, 16.09.1991, p. 897-903.

Research output: Contribution to journalArticle

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