A coupled optical enzyme assay for phosphopentomutase
β Scribed by Maria Grazia Tozzi; Roberta Catalani; Pier Luigi Ipata; Umberto Mura
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 401 KB
- Volume
- 123
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
Published assays for phosphopentomutase activity are based on acid lability differences between ribose l-phosphate and ribose S-phosphate. The present work describes a new method in which the isomerization of ribose 5-phosphate to ribose l-phosphate is followed spectrophotometrically at 265 nm by coupling it with the following two-stage enzymatic conversion: ribose l-phosphate + adenine S phosphate + adenosine (adenosine phosphorylase); adenosine + HZ0 -) inosine + NH3 (adenosine deaminase). The method has been used to show some properties of Escherichia coli phosphopentomutase.
π SIMILAR VOLUMES
The development of a coupled enzyme assay for the determination of isopenicilhn N synthetase activity in purified extracts from Cephalosporium acremonium was described. Isopenicillin N formed from its precursor, 8-(t-cr-aminoadipyl)-t-cysteinyl-o-valine (ACV), by the synthetase was hydrolyzed by @-l