Preparing
AST Assay Kit
The AST Test Kit is intended for the quantitative determination of aspartate aminotransferase (AST) activity. Cat.No: OttoBC127
Product Description
Aspartate aminotransferase (glutamate‑oxaloacetate‑transaminase) belongs to the transaminases, which catalyze the interconversion of amino acids and a‑keto acids by transfer of amino groups. Aspartate aminotransferase is commonly found in human tissue. 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, skeletal muscle, and kidneys. AST is present in both the cytoplasm and mitochondria of cells. In cases involving mild tissue injury, the predominant form of AST is that from the cytoplasm, with a smaller amount coming from the mitochondria. Severe tissue damage results in more of the mitochondrial enzyme being released. Elevated levels of the transaminases can signal myocardial infarction, hepatic disease, muscular dystrophy, and organ damage. The International Federation of Clinical Chemistry (IFCC) recommended in 1977 and 1980 standardized procedures for AST determination, including optimization of substrate concentrations, employment of TRIS* buffers, preincubation of combined buffer and serum to allow side reactions with NADH to occur, substrate start, and optional pyridoxal phosphate activation. In 2002 the IFCC confirmed their recommendation and extend it to 37°C. This method is derived from the IFCC reference method. *TRIS = Tris(hydroxymethyl)‑ aminomethane
Contents
UV test according to a standarrized method Sample and addition of R1 (buffer) Addition of R2 and start of reaction:
α‑ketoglutarate + L‑aspartate L‑ glutamate + oxaloasetate
AST is the enzyme which catalyzes this equilibrium reaction. The oxaloacetate in‑ crease is measured in a subsequent indicator reaction which is catalyzed by malate dehydrogenase.
oxalacetate + NADH + H+ L‑Malate + NAD+
In the second reaction, NADH is oxidized to NAD. The rate of decrease in NADH (Measured photometrically) is directly proportional to the rate of formation of oxaloasetate, and thus the AST activity.
Referanslar
1. Bergmeyer HU, Herder M, Rej R. Approved recommendation (1985) on IFCC methods for the measurement of catalytic concentration of enzymes. Part
2. IFCC Method for aspartate aminotransferase. J Clin Chem Clin Biochem 1986;24:49. 2. Glick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1 986;32:470‑474.
3. Greiling H, Gressner AM (Hrsg.). Lehrbuch der Klinischen Chemie und Pathobiochemie,3. Auflage. Stuttgart/New York: Schattauer Verlag, 1995
4. Thefeld W et al. Dtsch med Wschr 1974;99:343.
5. Tietz NW (Hrsg.). Clinical Guide to Laboratory Tests, 3. Auflage. Philadelphia, PA: WB Saunders, 1995:76‑77.
6. Wallnöfer H, Schmidt E, Schmidt FW (Hrsg.). Synopsis der Leberkrankheiten. Stuttgart: Georg Thieme Verlag, 1974.
7. Thomas L, Klein G. Neue vorläufige Normalbereiche für neun Serumenzyme. Deutsches Ärzteblatt 2006;103;Heft 7.
8. Schumann G et al. IFCC Primary Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes at 37°C – Part 4. Reference Procedure for the Measurement of Catalytic Activity Concentrations of Alanine Aminotransferase. Clin Chem Lab Med 2002;40(7):718–724.
9. Thefeld W, Hoffmeister H, Busch, E‑W, Koller PU, Vollmar J. Referenzwerte für die Bestimmungen der Transaminasen GOT und GPT sowie der alkalischen Phosphatase im Serum mit optimierten Standardmethoden. Dtsch Med Wschr 1974;99:343‑351.
10. Klein G, Lehmann P, Michel E, Regenauer H. Vergleich der IFCC‑Methoden für ALAT, ASAT und GGT bei 37°C mit den eingeführten Standardmethoden bei 25°C und 37°C. Lab Med 1994;18:403‑404.
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