A rapid nonchromatographic assay for aminopropyltransferases
| Autor: | David Leroy Anton |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
S-Adenosylmethionine
Biophysics Spermine Spermidine Synthase Biochemistry Substrate Specificity chemistry.chemical_compound Biosynthesis Transferases Escherichia coli Polyamines Chemical Precipitation Molecular Biology chemistry.chemical_classification Chromatography Substrate (chemistry) Cell Biology Spermidine Enzyme chemistry Charcoal Putrescine Amine gas treating Adsorption Polyamine |
| Zdroj: | Analytical Biochemistry. 156:45-47 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/0003-2697(86)90151-x |
| Popis: | Aminopropyltransferases are key enzymes in the biosynthesis of the polyamines spermidine and spermine. A procedure is described for assaying these enzymes by differential charcoal adsorption of 14C-labeled decarboxylated adenosylmethionine substrate from the labeled polyamine product. This assay is linear with time and enzyme concentration, and is suitable for use with a variety of amine acceptors. This procedure has the advantage, over those previously used, that it is extremely rapid yet very sensitive. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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