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A rapid and sensitive assay for tyrosine-3-monooxygenase based upon the release of 3H2O and adsorption of [3H]-tyrosine by charcoal
- Source :
- Life Sciences. 39:2185-2189
- Publication Year :
- 1986
- Publisher :
- Elsevier BV, 1986.
-
Abstract
- A rapid, simple and sensitive assay has been developed for tyrosine-3-monooxygenase, the enzyme catalyzing the rate-limiting step in catecholamine biosynthesis. The assay is based upon the release of 3H2O from 3H-[3,5]-L-tyrosine with adsorption of the isotopic substrate (and its metabolites) by an aqueous slurry of activated charcoal. This method routinely yields low blank values and is simpler than the procedure requiring the use of cation exchange columns to separate the isotopic substrate from the 3H2O formed during the hydroxylation reaction.
- Subjects :
- Chromatography
Aqueous solution
Tyrosine 3-Monooxygenase
Chemistry
Substrate (chemistry)
General Medicine
Tritium
General Biochemistry, Genetics and Molecular Biology
Hydroxylation
chemistry.chemical_compound
Adsorption
Activated charcoal
Charcoal
Methods
medicine
Animals
Tyrosine
General Pharmacology, Toxicology and Pharmaceutics
Activated carbon
medicine.drug
Subjects
Details
- ISSN :
- 00243205
- Volume :
- 39
- Database :
- OpenAIRE
- Journal :
- Life Sciences
- Accession number :
- edsair.doi.dedup.....4db34a49e49995d37fc04137d5280e2b