𝔖 Bobbio Scriptorium
✦   LIBER   ✦

A simple spectrophotometric assay for arogenate dehydratase

✍ Scribed by Suhail Ahmad; Roy A. Jensen


Publisher
Elsevier Science
Year
1987
Tongue
English
Weight
404 KB
Volume
163
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis


A simple spectrophotometric assay for arogenate dehydratase, tile enzyme that catalyzes the formation of L-phenylalanine from L-arogenate, is presented. The method couples the arogenate dehydratase reaction with that of an aromatic aminotransferase partially purified from Acinetobacter calcoaceticus. In the presence of 2-ketoglutarate, phenylpyruvate formation is measured at 320 nm at basic pH. The method was compared with two other methods already in use in our laboratory for arogenate dehydratase. The new method is simple, quick, fairly sensitive, and especially suitable for the screening of a large number of samples. o 1987 Academic FTes, Inc.


πŸ“œ SIMILAR VOLUMES


An assay for activity of arogenate dehyd
✍ Charles L. Shapiro; Roy A. Jensen; Karl A. Wilson; John R. Bowen πŸ“‚ Article πŸ“… 1981 πŸ› Elsevier Science 🌐 English βš– 341 KB

An improved method of assay is presented for arogenate dehydratase, an enzyme catalyzing the formation of t.-phenylalanine from L-arogenate. The improvement consists of the inclusion of a step in which arogenate is selectively oxidized using potassium permanganate prior to the measurement of phenyla

A spectrophotometric assay for cellobias
✍ D.L. Liu; C.C. Walden πŸ“‚ Article πŸ“… 1969 πŸ› Elsevier Science 🌐 English βš– 390 KB

Chemical methods for measuring cellobiase activity are based on increased reducing capacity, following conversion of cellobiose into glucose (l-3). The chemical methods are time consuming, of low sensitivity, and nonspecific. Enzymic methods use glucose oxidase to estimate the amount of glucose libe

A simple spectrophotometric assay for fu
✍ M.D. Hatch πŸ“‚ Article πŸ“… 1978 πŸ› Elsevier Science 🌐 English βš– 333 KB

A procedure is described for assaying fumarate hydratase by coupling malate formed from fumarate to NADP+ reduction via NADP malic enzyme. The procedure is much more sensitive than existing assay methods and circumvents problems particularly associated with the use of these methods for determining f