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Heterologous expression and characterization of a proxidomal ascorbate peroxidase from Populus tomentosa

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Abstract

The present study reported for the first time, cloning, expression and characteristics of a Proxidomal APX gene (PpAPX) from Populus tomentosa. The PpAPX gene encodes a protein of 287 amino acid residues with a calculated molecular mass of 31.58 kDa. The over-expressed recombinant PpAPX protein showed high activity towards the substrates ascorbate aicd (ASA) and H2O2. At fixed ASA concentrations, the K m and V max values were 0.12 ± 0.01 mM and 23.4 ± 4.2 mmol/min mg for H2O2. And at fixed H2O2 concentrations, the K m and V max values were 0.53 ± 0.04 mM and 20.0 ± 2.3 mmol/min mg for ASA.

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Acknowledgements

This work was jointly supported by the Key Project of Chinese Ministry of Education (no. 106039).

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Correspondence to Hai Lu.

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Lu, H., Han, RL. & Jiang, XN. Heterologous expression and characterization of a proxidomal ascorbate peroxidase from Populus tomentosa . Mol Biol Rep 36, 21–27 (2009). https://doi.org/10.1007/s11033-007-9147-6

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  • DOI: https://doi.org/10.1007/s11033-007-9147-6

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