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Ast (got) assay

Product Method Size Catalog Price Quantity
Ast (got) assay IFCC with P5P 4 x 90 tests AS2800 $205.59
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  • Format
    Mixing and diluting are automatically performed by the Dimension system
  • Assay Range
    7.39 - 1000 U/L
  • Working Stability 15-25 °C
    _
  • Working Stability 2-8 °C
    Stable to expiry
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Intended Use

For the quantitative in vitro determination of Aspartate Aminotransferase (AST) activity in serum or plasma. This product is suitable for use on the Siemens Dimension® analyzers.


Clinical Significance

The aminotransferases are a group of enzymes that catalyze the inter conversions of amino acids and α­oxoacids by transfer of amino groups. AST (aspartate aminotransferase or glutamate oxaloacetate transaminase) has been found in the cytoplasm and the mitochondria of cells that have been studied. In cases of mild tissue damage e.g. liver the predominant form of serum AST is that from the cytoplasm, with a smaller amount coming from the mitochondria.

Severe tissue damage will result in more mitochondrial enzyme being released.

AST is usually tested alongside ALT to diagnose liver damage. AST levels are sometimes compared directly to ALT and an AST/ALT ratio is calculated. This ratio may be used to distinguish between different causes of liver damage.

Extremely high levels of AST are associated with acute hepatitis and are usually due to viral infection. Levels can also be high as a result of drugs or other substances toxic to the liver. Levels are moderately high in chronic hepatitis or cirrhosis.

Elevated levels of AST can also signal myocardial infarction, muscular dystrophy and organ damage. Although heart muscle is found to have the most activity of the enzyme, significant activity has also been seen in the brain, liver, gastric mucosa, adipose tissue and kidneys of humans.


Principle

Aspartate aminotransferase (AST) catalyzes the transamination from L-aspartate to a-ketoglutarate, forming L-glutamate and oxaloacetate. The oxaloacetate formed is reduced to malate by malate dehydrogenase (MDH) with simultaneous oxidation of reduced nicotinamide adenine dinucleotide (NADH). The change in absorbance with time due to the conversion of NADH to NAD is directly proportional to the AST activity and is measured using a bichromatic (340, 700 nm) rate technique.


Available Applications

  • Dimension dedicated