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卡尔卡尔连续分光光度法测定腺苷脱氨酶活性的有效性。

Validity of the continuous spectrophotometric assay of Kalckar for adenosine deaminase activity.

作者信息

Tritsch G L

出版信息

Anal Biochem. 1983 Feb 15;129(1):207-9. doi: 10.1016/0003-2697(83)90070-2.

DOI:10.1016/0003-2697(83)90070-2
PMID:6859524
Abstract

Both adenosine and inosine obey Beer's law to 1.0 mM at 265 nm and pH 7.4 at 25 degrees C. Murphy et al. (1) claimed serious deviation from Beer's law above 200 microM for both substances, and concluded that the assay of adenosine deaminase activity based on recording spectrophotometric change at 265 nm as originally suggested by Kalckar produces anomalous results. The data herein presented show that this is not so, and that the large number of published studies of adenosine deaminase activity assayed by this method are indeed valid and should not be dismissed as artifactual as suggested by Murphy et al.

摘要

在25摄氏度、pH 7.4的条件下,腺苷和肌苷在265 nm波长处浓度达1.0 mM时均符合比尔定律。墨菲等人(1)称,这两种物质在浓度高于200 microM时严重偏离比尔定律,并得出结论:按照卡尔卡尔最初建议的在265 nm波长处记录分光光度变化来测定腺苷脱氨酶活性会产生异常结果。本文所呈现的数据表明并非如此,而且大量已发表的采用该方法测定腺苷脱氨酶活性的研究确实有效,不应像墨菲等人所暗示的那样被视为人为假象而不予理会。

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Validity of the continuous spectrophotometric assay of Kalckar for adenosine deaminase activity.卡尔卡尔连续分光光度法测定腺苷脱氨酶活性的有效性。
Anal Biochem. 1983 Feb 15;129(1):207-9. doi: 10.1016/0003-2697(83)90070-2.
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The pH dependence of spectral parameters for Kalckar's adenosine deaminase assay.卡尔卡腺苷脱氨酶测定中光谱参数的pH依赖性
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A critical reexamination of the continuous spectrophotometric assay for adenosine deaminase.对腺苷脱氨酶连续分光光度测定法的批判性重新审视。
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On the validity of continuous spectrophotometric assays for adenosine deaminase activity: a critical reappraisal.关于腺苷脱氨酶活性连续分光光度测定法的有效性:一项批判性重新评估。
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