Ad
related to: phosphoworks colorimetric atp assay protocol worksheet form g for 1
Search results
Results from the WOW.Com Content Network
ATP is quantified by measuring the light produced through its reaction with the naturally occurring firefly enzyme luciferase using a luminometer. The amount of light produced is directly proportional to the amount of ATP present in the sample. ATP tests can be used to: Control biological treatment reactors; Guide biocide dosing programs
ATP cleavage is tightly linked to substrate translocation, as the energy for the substrate translocation is derived from ATP hydrolysis. ATP hydrolysis yields inorganic phosphate (Pi), which can be measured by a simple colorimetric reaction. The amount of Pi liberated is directly proportional to the activity of the transporter. [1]
[1] The NBT/BCIP reaction is also used for colorimetric/ spectrophotometric activity assays of oxidoreductases . One application is in activity stains in gel electrophoresis , such as with the mitochondrial electron transport chain complexes.
Colorimetric analysis is a method of determining the concentration of a chemical element or chemical compound in a solution with the aid of a color reagent. It is applicable to both organic compounds and inorganic compounds and may be used with or without an enzymatic stage.
Colorimetric assays use reagents that undergo a measurable color change in the presence of the analyte. They are widely used in biochemistry to test for the presence of enzymes, specific compounds, antibodies, hormones and many more analytes. For example, para-Nitrophenylphosphate is converted into a yellow product by alkaline phosphatase enzyme.
Direct versus coupled assays. Coupled assay for hexokinase using glucose-6-phosphate dehydrogenase. Even when the enzyme reaction does not result in a change in the absorbance of light, it can still be possible to use a spectrophotometric assay for the enzyme by using a coupled assay. Here, the product of one reaction is used as the substrate ...
The discovery of dephosphorylation came from a series of experiments examining the enzyme phosphorylase isolated from rabbit skeletal muscle. In 1955, Edwin Krebs and Edmond Fischer used radiolabeled ATP to determine that phosphate is added to the serine residue of phosphorylase to convert it from its b to a form via phosphorylation. [3]
The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [2] spectroscopic analytical procedure used to measure the concentration of protein in a solution. The reaction is dependent on the amino acid composition of the measured proteins.
Ad
related to: phosphoworks colorimetric atp assay protocol worksheet form g for 1