| 徐凡，吴媚.烟草谷草转氨酶纯化及部分酶学性质分析[J].广东农业科学,2013,40(10):146-148 |
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烟草谷草转氨酶纯化及部分酶学性质分析 |
| Purification of glutamic-oxaloacetic transaminase from tobacco and part of its characteristics |
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| DOI： |
| 中文关键词: 烟草 谷草转氨酶 纯化 酶学性质 |
| 英文关键词: tobacco glutamic-oxaloacetic transaminase purification enzymatic characteristics |
| 基金项目:/ |
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| 摘要点击次数: 1348 |
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| 中文摘要: |
| 采用硫酸铵沉淀，SephadexG-100层析和DEAE-Sepharose纯化烟草中的谷草转氨酶（GOT），并对酶的最适温度、最适pH值和金属离子对酶活力的影响等进行了研究。结果表明，该酶最适反应温度为37℃，最适pH范围为8.5~9.0，Mn2+、Zn2+，Fe2+对GOT起激活作用，最佳氨基供体为L-天冬氨酸，酶促反应的Vmax为0.575μmol/L·min袁L-天冬氨酸和a-酮戊二酸的米氏常数分别为0.929μmol/L和0.105μmol/L；研究还表明，GOT不能催化吡哆胺转变为吡哆醛，证明在植物体内有另外一种转氨酶催化该反应，为植物体内VB6代谢途径的进一步研究提供了依据。 |
| 英文摘要: |
| Glutamic-oxaloacetic transaminase was purified from tobacco by ammonium sulfate, DEAE-Sepharose Fast Flow ion exchange chromatography, Sephadex G -100 gel filtration. And the characteristics were intensively studied. The optimum reaction conditions of GOT were gained: temperature 37益, pH 8.5~9.0. Mn2+, Zn2+, Fe2+ could activate the activity of GOT, the best amino donor was L-Aspartate. The maximum reaction rate of the enzymatic reactions was 0.575 滋mol/L窑min, and the Michaelis constant of LAspartate and a-ketoglutarate were 0.929 滋mol/L and 0.105 滋mol/L. The study also showed that GOT couldn't catalyze the reaction between pyridoxine and pyridoxal, which could prove that there was another transaminase to catalyze the reaction in higher plants. |
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