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固定化酶微观活性定位的X射线微区分析
引用本文:丁良,姚子华.固定化酶微观活性定位的X射线微区分析[J].光谱学与光谱分析,2004,24(9):1136-1139.
作者姓名:丁良  姚子华
作者单位:河北省职工医学院,河北,保定,071002;河北大学理化分析中心,河北,保定,071002;河北省职工医学院,河北,保定,071002
摘    要:利用X射线微区分析,对共价法得到的固定化L—天门冬酰胺酶的活性进行了分析。L—天门冬酰胺作为底物,MgCl2作为捕捉剂,底物经L-天门冬酰胺酶催化分解产生氨,后者和捕捉剂反应产生沉淀,可以确定固定化L-天门冬酰胺酶的催化活性部位。结果表明:大孔树脂载体,酶活较高,活性L-天门冬酰胺酶分布较均匀。并得到了固定化L-天门冬酰胺酶的活性定位的最佳条件。并对不同结构载体固定化酶活性进行了研究。

关 键 词:X射线微区分析  固定化L-天门冬酰胺酶  大孔吸附树脂  酶活
文章编号:1000-0593(2004)09-1136-04
修稿时间:2002年11月25

X-Ray Microanalysis of the Activity of Immobilized L-Asparaginase
DING Liang ,YAO Zi-hua . Hebei College of Continuing Medical Education,Baoding ,China . Research Center of Physical and Chemical Analysis,Hebei University,Baoding ,China.X-Ray Microanalysis of the Activity of Immobilized L-Asparaginase[J].Spectroscopy and Spectral Analysis,2004,24(9):1136-1139.
Authors:DING Liang    YAO Zi-hua Hebei College of Continuing Medical Education  Baoding  China Research Center of Physical and Chemical Analysis  Hebei University  Baoding  China
Institution:Hebei College of Continuing Medical Education, Baoding 071002, China.
Abstract:The localization of activity of immobilzed L-asparaginase by covalent binding was studied by X-ray microanalysis. Asparagine and MgCl 2 served as substrate and capture agent respectively. Substrate was catalysed by immobilized L-asparaginase to produce NH 3, and NH 3 was captured by MgCl 2 to form precipitate MgNH 4PO 4. Precipitae was deposited on active site of immobilized L-asparaginase. The results show that the macroporous resins of immobilized L-asparaginase has greater enzyme activity, while distribution of activated enzyme was uniform. Most of activated enzyme was immobilized on the macroporous resins. The optimum condition of localization of activity of immobilized L-asparaginase was studied.
Keywords:X-ray microanalysis  Immobilized L-asparaginase  Macroporous resins  Enzyme activity
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