A continuous, automated assay for the measurement of acetate kinase activity in Escherichia co/i is described. The assay system consists of three steps: continuous sonication, acetate kinase catalyzed production of ATP, and subsequent measurement of ATP concentration. Complete extraction of acetate
Continuous Enzymatic Assay for Phosphorylase Kinase in a Monocascade Enzyme System
β Scribed by Natalya B. Livanova; Iraida E. Andreeva; Valentina F. Makeeva; Boris I. Kurganov
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 138 KB
- Volume
- 244
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
An easy, rapid, and accurate enzymatic assay method for L-serine was established involving two enzymes, serine-glyoxylate aminotransferase (SGAT, EC 2.6.1.45) and hydroxypyruvate reductase (HPR, EC 1.1.1.81), in the serine pathway of the methylotrophic bacterium, Hyphomicrobium methylovorum (IFO 141
## Abstract The activity of __Chromobacterium viscosum__ lipase (glycerolβester hydrolase, EC 3.1.1.3) entrapped in AOT/isooctane reverse micelles was significantly increased by the addition of short chain polyethylene glycols (PEGs) or methoxypolyethylene glycols (MPEGs) for the hydrolysis of oliv
A new method for assaying the enzymes N\*-acetyl-L-omithine:L-glutamate N-acetyltransferase (EC 2.3.1.35) and acetyl-coenzyme A:~-glutamate N-acetyltransferase (EC 2.3.1.1) has been designed. This assay system is based on the separation of N-['4C]acetylghuamate from N-[ "'Clacetylomithine or [?Z]ace