A simple procedure is described for assaying phosphoenolpyruvate carboxykinase in the direction of oxaloacetate decarboxylation by following the decrease in oxaloacetate absorbance. The procedure offers a means of measuring the activity of this enzyme in its physiological direction in unfractionated
A simple spectrophotometric assay for fumarate hydratase in crude tissue extracts
โ Scribed by M.D. Hatch
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 333 KB
- Volume
- 85
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
โฆ Synopsis
A procedure is described for assaying fumarate hydratase by coupling malate formed from fumarate to NADP+ reduction via NADP malic enzyme. The procedure is much more sensitive than existing assay methods and circumvents problems particularly associated with the use of these methods for determining fumarate hydratase in crude tissue extracts.
Methods
Biochemicals and reagent enzymes, including pigeon liver NADP malic enzyme [malate dehydrogenase (decarboxylating), (NADP+), EC1 . 1.1.40], were obtained from Sigma Chemical Co. (St. Louis, MO). Partially purified Zea mays (corn) leaf NADP malic enzyme, freed of fumarate hydratase
๐ SIMILAR VOLUMES
All the current methods available for analyzing the acetylcholinesterase (ACHE) molecular forms are time consuming and require the use of expensive equipment. We have found that by using the differential inactivation of globular (G4 + Gt) and asymmetric AChE forms by high Mg 2+ concentration, we ca
Superoxide dismutase (EC 1.15.1.1) has been assayed by a spectrophotometric method based on the inhibition of a superoxide-driven NADH oxidation. The assay consists of a purely chemical reaction sequence which involves EDTA, Mn(II), mercaptoethanol, and molecular oxygen, requiring neither auxiliary