AST/GOT Chemistry Reagents


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AST/GOT Chemistry Reagents


Aspartate aminotransferase (AST/GOT) catalyzes the transfer of the amino group from aspartate to oxoglutarate with the formation of glutamate and oxalacetate. The latter is reduced to malate by
malate dehydrogenase (MDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH).

The reaction is monitored kinetically at 340 nm by the rate of decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to the activity of AST present in the sample.

Product Overview

  • IFCC standards: This test has been formulated according the standardized method
    described by IFCC. Clin Chem Lab Med 2002; 40(7) : 718-7242
  • UV enzymatic method
  • Kinetic
  • AST/GOT 3 x 100ml
  • Storage: at 2-8ºC

R1 AST substrate TRIS buffer 121 mmol/L pH 7.8, L-aspartate
362 mmol/L, malate dehydrogenase  460 U/L.

R2 AST coenzyme:  NADH 1.3 mmol/L, 2-oxoglutarate 75

Working reagent: Mix 4 mL of R1 + 1 mL of R2. Stable for 4 weeks
at 2-8ºC. Protect from light.

Serum, EDTA or heparinized plasma free of hemolysis.
AST is stable in serum or plasma 24 hours at room temperature and for 1 week at 2-8ºC.


  • Photometer or spectrophotometer with a thermostatic cell compartment set at 30/37ºC, capable of reading at 340 nm.
  • Stopwatch, strip-chart recorder or printer. Cuvettes with 1-cm pathlength.
  • Pipettes to measure reagent and samples.

AST/GOT Chemistry Reagents per box