Equations are given for minimizing the cost and calculating the maximum practical rates for coupled assays when two or more coupling enzymes are involved, and a lag of a predetermined size can be tolerated. The lag caused by obligatory mutarotation of an intermediate is also calculated.
Enzyme-Coupled Assays for Proteases
β Scribed by Brian E. Cathers; John V. Schloss
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 104 KB
- Volume
- 241
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
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 co
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
## D-Alanine (D-Ala ) is a ubiquitous constituent of bacterial cell walls. Assays for D-Ala can be used to investigate several aspects of cell wall biosynthesis and the effects of antibiotics on this process. High-sensitivity fluorescent assays for D-Ala were developed in a microtiter plate format