| Cat# | Product Name | Price |
|---|---|---|
| Kit-2452 | Creatine Kinase Assay Kit | Inquiry |
Creatine kinase (CK) is an enzyme widely present in muscles, heart, brain, and other tissues. Its function in muscle cells is to catalyze creatine phosphate and ATP to creatine and phosphate. When muscles are damaged, CK is released into the bloodstream, so the measurement of CK can be used to measure the degree of muscle damage.
The biological activity of Creatine kinase is to catalyze the formation of products creatine and phosphate from the substrate creatine phosphate and ATP.
The main principle of activity determination methods is based on enzyme catalyzed reactions. One common method for measuring creatine kinase activity is to use NADH H as a substrate to measure the changes in NADH consumption under different conditions, thereby inferring the level of enzyme activity.
In addition, there are two measurement methods as follows:
Cobalt colorimetric method: Under pH 10 conditions, creatine phosphate combines with sodium 2,4,6-trinitrobenzenesulfonate to form a staining product, and the colorimetric value of the product is measured by spectrophotometry. This method is easy to operate, with stable results and no interference from interfering substances. But this method requires a larger volume and reaction time.
AMP chemiluminescence method: When the content of creatine phosphate and ATP is equal, creatine kinase will quickly catalyze the degradation of creatine phosphate, producing AMP. The conversion of AMP to ATP requires the consumption of ATP. Finally, the luciferin binds with ATP to generate a light signal, which is detected by a fluorescence photometer. This method is extremely sensitive and requires a short amount of time.
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