| Cat# | Product Name | Price |
|---|---|---|
| Kit-0082 | Alanine Transaminase Assay Kit | Inquiry |
| Kit-0083 | ALT Assay Kit | Inquiry |
| Kit-0084 | ALT Fluorometric Assay Kit | Inquiry |
| Kit-2209 | Alanine Aminotransferase Activity Colorimetric/Fluorometric Assay Kit | Inquiry |
Alanine aminotransferase (ALT, also known as SGPT) is an enzyme present in various cell types, including liver, spleen, kidney, and lung cells, primarily responsible for transferring amino acids. ALT is usually used to assess the health of the liver, as when liver cells are damaged, they release ALT into the bloodstream.
ALT mainly exists in liver cells, and when liver cells are damaged, ALT will be released into the bloodstream. Therefore, ALT is an important indicator of liver function. When the liver is healthy, ALT levels are usually very low, while when the liver is damaged, ALT levels will increase.
The activity determination method of ALT is usually based on its catalytic substrate conversion reaction, which involves substrate glutamic acid and α- Ketoacetic acid is converted into oxalic acid and pyruvic acid through ALT catalysis, and the reaction formula is as follows:
L-alanine 2-oxoglutarate ↔ pyruvate L-glutamate
This reaction can be determined using various methods, among which the most commonly used methods include:
The principle of this method is to use enzyme catalysis to combine glutamic acid with α- Ketoacetic acid is converted into oxalic acid and pyruvic acid, while generating NADH. Use the absorbance changes of NADH to measure ALT activity. In this method, certain indicators such as dimeric pyridine ketone and 4-aminoantipyrine can increase the absorbance of NADH and color it, thereby increasing the detection sensitivity of the reaction.
High performance liquid chromatography (HPLC) can be used to separate and quantify glutamic acid and α- Ketoacetic acid, oxalic acid, and pyruvic acid. This method uses specific chromatographic columns to separate substrates and products, and then uses specific detectors to detect glutamate and α- Determine the activity of ALT by changing the concentration of ketovaleric acid. This method has the advantages of high sensitivity, accuracy, and reproducibility, but requires more complex equipment and high costs.
Immunological methods can use some commercially available antibodies to detect the activity of ALT. The principle of this method is to label the enzyme substrate with an antibody. When ALT is present, the substrate binds to the antibody and forms a complex. Then, specific peptide chemicals are used to convert the complex into a staining substance. Finally, the activity of ALT is measured by detecting the optical density of the staining substance. This method has the advantages of simple operation, fast sensitivity, and easy automation, but it is relatively expensive.
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