A sensitive fluorometric assay for dopamine-β-hydroxylase activity by high-performance liquid chromatography
✍ Scribed by Hiroaki Matsui; Noriko Kato; Chosaburo Yamamoto; Keisuke Fujita; Harutada Sakai; Toshiharu Nagatsu
- Book ID
- 115767177
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 380 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-2944
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
As a model for the assay of enzyme activity by high-performance liquid chromatography, a simple, sensitive and specific fluorescence assay for dopamine P-hydroxylase (DBH) activity was devised using o-phthalaldehyde as reagent. Tyramine was used as a substrate and was incubated under optimal conditi
A rapid sensitive method for the quantification of in vitro HIV-protease activity has been developed on the basis of the endoproteolytic conversion of N-Dns-SQ-NYPIV to N-Dns-SQNY. The use of the N-dansyl group as a fluorescence label was shown to not significantly alter the apparent kinetic paramet
The activity of peptidylarginine deiminase (PAD) has generally been assayed by a colorimetric method using N-benzoyl-L-arginine ethyl ester (BAEE) and Nbenzoyl-L-arginine (Bz-L-Arg) as the substrates. The widespread occurrence of citrulline and urea in tissues makes use of this method difficult, esp
A time-resolved assay of dopamine /3-hydroxylase (EC 1.14.17.1) activity utilizing highpressure liquid chromatography is described. The conversion of tyramine to octopamine by the enzyme was used as a standard reaction. The analytical separation of the assay substrate and product employed a reversed