收稿日期: 2003-07-10
修回日期: 2003-09-09
网络出版日期: 2004-05-10
基金资助
国家自然科学基金 (29701005);中国科学院重大项目 (KJ951A150402)资助
Purification and Characterization of UGPase
Received date: 2003-07-10
Revised date: 2003-09-09
Online published: 2004-05-10
经4步分离纯化的Apocynaceae植物培养细胞尿苷二磷酸葡萄糖焦磷酸化酶(UGPase)的比活为2049Umg，与细胞粗提液相比，活力提高97倍，活力回收率为21%，可直接用于尿苷二磷酸葡萄糖(UDPG)的合成，并且储存稳定性很好。UGPase的最适pH值为72，UGPase的最适温度为37℃左右。Mg2+是UGPase发挥活力所必需的。高浓度UTP和Glc6P均能抑制UGPase的活力。
关键词： 尿苷二磷酸葡萄糖焦磷酸化酶; 纯化; 表征; 比活
祁超 . Apocynaceae系细胞尿苷二磷酸葡萄糖焦磷酸化酶的纯化和表征[J]. 中国科学院大学学报, 2004 , 21(3) : 345 -351 . DOI: 10.7523/j.issn.2095-6134.2004.3.010
After isolation and purification of four steps, specific activity of UGPase from Apocynaceae cell is 204 9 U/mg. Compared with crude cell culture, specific activity is 97 times, and recovery yield is 21%. UGPase can be used in the synthesis of UDPG, and it has higher stability. The best available pH of UGPase is about 7 2, the best available temperature about 37℃. Mg2+ is necessary for UGPase to use. The high concentration of UTP and Glc 6 P can inhibit the activity of UGPase.
Key words： UGPase; purification; characterization; specific activity
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