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毛白杨近端抗坏血酸过氧化物酶的异源表达与特性分析

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

作者信息

Lu Hai, Han Rui-Li, Jiang Xiang-Ning

机构信息

Beijing Forestry University, Beijing Haidian district, Beijing 100083, People's Republic of China.

出版信息

Mol Biol Rep. 2009 Jan;36(1):21-7. doi: 10.1007/s11033-007-9147-6. Epub 2007 Sep 27.

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 H(2)O(2). 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 H(2)O(2). And at fixed H(2)O(2) concentrations, the K (m) and V (max) values were 0.53 +/- 0.04 mM and 20.0 +/- 2.3 mmol/min mg for ASA.

摘要

本研究首次报道了毛白杨近端抗坏血酸过氧化物酶基因(PpAPX)的克隆、表达及特性。PpAPX基因编码一个由287个氨基酸残基组成的蛋白质,计算分子量为31.58 kDa。过表达的重组PpAPX蛋白对底物抗坏血酸(ASA)和H₂O₂表现出高活性。在固定ASA浓度下,H₂O₂的Km和Vmax值分别为0.12±0.01 mM和23.4±4.2 mmol/min mg。在固定H₂O₂浓度下,ASA的Km和Vmax值分别为0.53±0.04 mM和20.0±2.3 mmol/min mg。

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