THE PH-DEPENDENCE OF SPECTRAL PARAMETERS FOR KALCKARS ADENOSINE-DEAMINASE ASSAY
THE PH-DEPENDENCE OF SPECTRAL PARAMETERS FOR KALCKARS ADENOSINE-DEAMINASE ASSAY
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DOI：
10.1016/0003-2697(87)90593-8
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发表时间：
1987-11-01
影响因子：
2.9
通讯作者：
CERCIGNANI, G
中科院分区：
文献类型：
--
作者：
CERCIGNANI, G
最佳监测波长和微分毫摩尔消光系数（m Δ.（.）用于测定腺苷脱氨酶在几种底物上催化的反应的速率，已被研究为pH在6.5至12范围内的函数。在某些情况下，发现的值与生物化学文献中引用的值不同。pH对m Δ的影响- 是的值显示出与反应中产物和/或底物的酸碱性质明显相关。实验数据在大多数情况下用于导出描述m Δ的pH依赖性的分析函数。你...对于在pH6.5下腺苷向肌苷的转化，使用以下m Δ值。你..+-.在263 nm处获得SE：8.27 ± 0.001。0.02;在264 nm处，8.36 ±。0.02;在265 nm处，8.27 ±。0.03.这些代表作为pH值的函数的绝对最大值。
Optimal monitor wavelengths and differential millimolar extinction coefficients (m.DELTA..epsilon.) for rate determination of reactions catalyzed by adenosine deaminases on several substrates have been investigated as a function of pH in the range from 6.5 to 12. The values found are in some cases at variance with those quoted in the biochemical literature. The effect of pH on m.DELTA..epsilon. values is shown to be clearly related to acid-base properties of product and/or substrate in the reaction. Experimental data are in most cases used to derive analytical functions describing the pH dependence of m.DELTA..epsilon.. For the conversion of adenosine to inosine at pH 6.5, the following values of m.DELTA..epsilon..+-.SE were obtained: at 263 nm, 8.27 .+-. 0.02; at 264 nm, 8.36 .+-. 0.02; at 265 nm, 8.27 .+-. 0.03. These represent absolute maximal values as a function of pH.