Kinetic investigations on adenosine deaminase from calf intestinal mucosa by spectrophotometric monitoring of the reaction at 264, 270, or 228 nm show that this method does not produce artifactual inhibition by substrate excess up to 0.7 mM concentration, when either adenosine or 2'-deoxyadenosine a
Validity of the continuous spectrophotometric assay of Kalckar for adenosine deaminase activity
โ Scribed by George L. Tritsch
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 172 KB
- Volume
- 129
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
โฆ Synopsis
Both adenosine and inosine obey Beer's law to 1.0 mM at 265 nm and pH 7.4 at 25ยฐC. Murphy et al. ( 1) claimed serious deviation from Beer's law above 200 CM 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.
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