A simple, rapid, and sensitive fluorometric assay for measuring the activity of tyrosine hydroxylase is described. The enzyme activity is detected by converting tyrosine to 3,4-dihydroxyphenylalanine (dopa), which is then subjected to conversion to the highly fluorescent product by the trihydroxyind
A simple and sensitive assay for dopamine-β-hydroxylase
✍ Scribed by Tong Hyub Joh; Robert A. Ross; Donald J. Reis
- Publisher
- Elsevier Science
- Year
- 1974
- Tongue
- English
- Weight
- 349 KB
- Volume
- 62
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
A simple, rapid, and highly sensitive radiochemical assay for measuring the activity of dopamine+hydroxylase in tissues and serum is described. Enzyme activity is detected by converting [l-'"Cltyramine to [l-"Cloctopamine which is then subjected to periodate cleavage to form ["Clformamide. This radiolabeled product is oxidized to "CO, by addition of permanganate and the "CO, is trapped and counted. The assay is simple and sensitive, it can linearly detect enzyme in all tissues with a wide range of activity, it uses maximal concentration of substrate, and it requires the addition of only one concentration of EM1 to block endogenous inhibitor(s) in different tissues or enzyme concentrations.
📜 SIMILAR VOLUMES
Recent studies in this laboratory (1, 2) have revealed new information about the mechanism of the phenylalanine hydroxylase reaction. Briefly, these experiments show that during hydroxylation the para substituent of the substrate, phenylalanine, migrates and appears on the meta position(s) of the pr
## O-O activation / C-H activation The three-dimensional aspects of the chemistry of dopamine β-hydroxylase (DBH) was studied through a conformationally-restricted substrate analog approach. We found that the DBH-catalyzed hydroxylation of 2-aminoindane (1) exclusively produced the trans-(1S,2S)-2-