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
A critical reexamination of the continous spectrophotometric assay for adenosine deaminase
β Scribed by Joe Murphy; David C. Baker; Cynthia Behling; Russell A. Turner
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 809 KB
- Volume
- 122
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Both adenosine and inosine obey Beer's law to 1.0 mM at 265 nm and pH 7.4 at 25Β°C. 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 ori
We developed a specific spectrophotometric assay for the quantitative determination of phospholipase D-catalyzed transphosphatidylation activity. The assay measures p-nitrophenol liberated by phospholipase D-catalyzed reaction of phosphatidyl-p-nitrophenol and ethanol in an aqueous-organic emulsion