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[1]孙艳,王静,杨海麟,等.细菌黄嘌呤氧化酶的稳定性[J].生物加工过程,2009,7(02):53-56.
　SUN Yan,WANG Jing,YANG Hai-lin,et al.Stability of xanthine oxidase from Arthrobacter[J].Chinese Journal of Bioprocess Engineering,2009,7(02):53-56.
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细菌黄嘌呤氧化酶的稳定性
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《生物加工过程》[ISSN:1672-3678/CN:32-1706/Q]

卷:
7
期数:
2009年02期
页码:
53-56
栏目:
出版日期:
2009-03-30

文章信息/Info

Title:
Stability of xanthine oxidase from Arthrobacter
文章编号:
1672-3678(2009)02-0053-04
作者:
孙艳; 王静; 杨海麟; 王武
江南大学 工业生物技术教育部重点实验室,无锡 214122
Author(s):
SUN Yan;  WANG Jing;  YANG Hai-lin;  WANG Wu
The Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi 214122, China
关键词:
黄嘌呤氧化酶; 稳定性; 谷氨酸; 天冬氨酸
分类号:
Q554
文献标志码:
A
摘要:
研究pH、温度、金属离子和一些添加剂对黄嘌呤氧化酶稳定性的影响。结果表明：黄嘌呤氧化酶在pH 4.5～7.5 的范围内较稳定；反应最适温度为37 ℃。在常温25～35 ℃该酶比较稳定，经45 ℃处理2 h，可保持50%左右，不同种类、不同浓度的金属离子对黄嘌呤氧化酶活性表现出程度不同的激活或抑制作用；添加谷氨酸和天门冬氨酸，能有效提高黄嘌呤氧化酶的存放稳定性。


参考文献/References:

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［3］Pfeffer K D, Huecksteadt T P, Hoidal J R. Xanthine dehydrogenase and xanthine oxidase activity and gene expression in renal epithelial cells:cytokine and steroid regulation[J].Immunol,1994,153:1789-1795.
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［12］李忠琴,许小平,杨海麟，等. 辣根过氧化物酶分光光度法测定黄嘌呤氧化酶的活性[J]. 分析化学, 2006, 34(6):821-824.
Li Zhongqin, Xu Xiaoping, Yang Hailin, et al. Spectrophotometric determination of activity of xanthine xxidase by horseradish peroxidas[J]. Chinese Journal of Analytical Chemistry,2006,34(6):821-824.


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备注/Memo

备注/Memo:
收稿日期：2008-04-16
基金项目：工业微生物教育部重点实验基金资助项目（KLIB-KF200502）
作者简介：孙艳(1979—)，女，江苏连云港人，博士研究生，研究方向：酶工程；王武(联系人)，教授，博士生导师，E-mail:wangwu@jiangna.edu.cn
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