AST/GOT Chemistry Reagents

AST/GOT Chemistry Reagents PRINCIPLE 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 2-8?C REAGENT COMPOSITION 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 REAGENT PREPARATION Working reagent: Mix 4 mL of R1 + 1 mL of R2. Stable for 4 weeks at 2-8?C. Protect from light. SAMPLES 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 2-8?C. MATERIALS REQUIRED Photometer or spectrophotometer with a thermostatic cell compartment set at 30/37?C, 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