The use of [14C]aspartate of high specific activity and thin-layer chromatography on polyethyleneimine cellulose for the separation of carbamoyl aspartate from aspartate has enabled the measurement of aspartate carbamoyltransferase and carbamoyl phosphate synthase activities and carbamoyl phosphate
A radioisotope method for assays of amylomaltase and D-enzyme
โ Scribed by Sukumar Medda; Eric E. Smith
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 529 KB
- Volume
- 138
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
โฆ Synopsis
A method has been developed for the assay of amylomaltase based on the incorporation of a [14C]glucose moiety of uniformly 14C-labeled maltose into a maltodextrin fraction insoluble in aqueous ethanol. The presence of dextrin at a high concentration greatly enhances [14C]glucose incorporation and serves to minimize interference with the assay by contaminating enzymes that hydrolyze substrates and products in the assay mixture. Since a number of other enzymes are capable of forming glucose in the assay mixture, the 14C incorporation is a more specific method of enzyme assay than are previously reported assays based on glucose release.
๐ SIMILAR VOLUMES
Insoluble dye-protein complexes offer many advantages when used as substrates for proteolytie enzymes. The proteolytic split products can be separated from the starting substrat.e conveniently by filtration, and the concentration of the soluble colored products of hydrolysis can easily be measured a
We developed a specific spectrophotometric assay for the quantitative determination of phospholipase D-catalyzed transphosphatidylation activity. The assay measures p-nitrophenol liberated by phospholipase D-catalyzed reaction of phosphatidyl-p-nitrophenol and ethanol in an aqueous-organic emulsion