| 间羟苯甲酸4－羟化酶纯化及部分性质研究 |
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| 引用本文： | 陈瑞,细川桂一.间羟苯甲酸4－羟化酶纯化及部分性质研究[J].生物化学与生物物理进展,1996,23(4):337-342. |
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| 作者姓名： | 陈瑞 细川桂一 |
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| 作者单位： | 首都医科大学生物化学教研室;日本川崎医科大学生物化学教研室 |
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| 摘 要： | 经超声破碎、硫酸铵分级沉淀、凝胶过滤、磷酸钙胶层析和离子交换层析等步骤, 从Comamonas testosteroni菌株中获得了SDS-PAGE单一条带, 相对分子质量为62×103的间羟苯甲酸4-羟化酶比活提高21倍, 产率为30%.此酶为FAD加单氧酶, 催化间羟苯甲酸转变为3,4二羟苯甲酸.
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| 关 键 词： | 间羟苯甲酸4－羟化酶 纯化 性质 丛毛单孢菌 |
| 收稿时间： | 1995/9/25 0:00:00 |
Purification and Partial Characterization of meta-Hydroxybenzoate Hydroxylase |
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| Chen Rui and Keiichi Hosokawa.Purification and Partial Characterization of meta-Hydroxybenzoate Hydroxylase[J].Progress In Biochemistry and Biophysics,1996,23(4):337-342. |
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| Authors: | Chen Rui and Keiichi Hosokawa |
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| Institution: | Department of Biochemistry, Capital University of Midical Sciences;Department of Biochemislry, Kawasaki Medical School |
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| Abstract: | The m-hydroxybenzoate hydroxylase (MOB4-HOase) with 62 000 relative molecular mass from Comamonas testosteroni was purified to homogeneity upon SDS-PAGE by using sonic crushing, ammonium sulfate fractionation, molecular sieve chromatography, calcium phosphate gel chromatography and ion exchange chromatography. MOB4-HOase has been purified about 21 fold in specific activity with about 30% yield. This enzyme is a FAD-monooxygenase to catalyze m-hydroxybenzoate to protocatechuic acid. |
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| Keywords: | meta-hydroxybenzoate4- Hydroxylase purification characterization Comamonas testosteroni |
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