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
Assay of β-Carotene 15,15′-Dioxygenase Activity by Reverse-Phase High-Pressure Liquid Chromatography
✍ Scribed by Alexandrine During; Akihiko Nagao; Chimaki Hoshino; Junji Terao
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 138 KB
- Volume
- 241
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
High-pressure liquid chromatography (hplc) of N-acetylglucosamine (GlcNAc) and galactosamine (GalNAc) containing carbohydrates was performed on several reverse-phase silica columns. Nanomolar level detection was accomplished using far uv-absorbance monitoring. Baseline separations of the (Y and fl a
In this paper we present an HPLC method developed for quick activity and specificity analysis of serine proteinases. The method applies a carefully designed peptide library in which the individual components differ only at the potential cleavage site for enzymes. The library has seven members repres
plasma since aglycones of the drug and metabolites are not well resolved and elute near the solvent front, where there are high levels of nonspecific fluorescence due to plasma constituents. Aglycone separation is not a problem in the in uitro assays since there are few interfering substances. Sepa