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\ p None B a = c @ = Z ?N*8 X" 1 Arial1 Arial1 Arial1 Arial1 Arial1 Arial1 Arial General ` f Table_2 ' ' Analyte / Acronym Labtest Reference' Method name and summary Alanine aminotransferase/ALT 108 UV-IFCC:ALT specifically catalyzes the transfer of the amine group from alanine to ketoglutarate, with glutamate and pyruvate formation. Pyruvate is reduced to lactate by lactate dehydrogenase (LDH), while coenzyme NADH is oxidized to NAD. The absorbance reduction at 340nm or 365nm, as a result of NADH oxidation, is monitored photometrically and directly proportional to the ALT activity in the sample. Aspartate aminotransferase / AST 109-2 Kinetic UV: AST specifically catalyzes the transfer of the amine group from aspartic acid to ketoglutarate with glutamate and oxaloacetate formation. Oxalacetate is reduced to malate through the action of malate dehydrogenase (MDH), while the NADH coenzyme is oxidized to NAD. The reduction of the absorbance at 340 or 365nm, due to NADH oxidation, is monitored photometrically and directly proportional to the AST activity in the sample. Alkaline phosphatase/ALP 40\ Modified Roy: Serum alkaline phosphatase hydrolyzes thymolphthalein monophosphate by releasing thymolphthalein, which is blue in an alkaline medium. The formed color, which is directly proportional to enzymatic activity, is measured at 590nm. The final reaction product consists of a mixture of blue and the substrate’s color itself. Cholesterol/CHOL 76-2 Enzymatic hydrolysis /oxidation (Trinder): Cholesterol esters are hydrolyzed by cholesterol esterase to free cholesterol and fatty acids. Cholesterol free is oxidized by cholesterol oxidation to cholest-4-em-one and hydrogen peroxide. In the presence of peroxidase and hydrogen peroxide, phenol and 4-aminoantipyrine are oxidized to form antipyrilquinonimine with maximum absorbance at 500nm. Creatine kinase/CK 117 UV-IFCC: CK catalyzes the dephosphorylation of creatine phosphate to produce adenosine triphosphate (ATP), which reacts with glucose in the presence of hexokinase (HK) to form glucose-6-phosphate which, in the presence of glucose-6-phosphate dehydrogenase (G-6- PDH), is oxidized to 6-phosphogluconate (6-PG) and reduces NAD to NADH. The rate of increased absorbance at 340nm is proportional to the CK activity in the sample. - g l u t a m y l t r a n s f e r a s e / G G T 105-2F Modified Szasz: GGT catalyzes the transfer of the glutamyl group of L-γ-glutamyl-3-carboxy-4-nitroanilide to glycylglycine by forming L-γ-glutamylglycylglycine and p-nitroaniline. The amount of p-nitroaniline, which has a high absorbance at 405nm, is directly proportional to the GGT activity in the sample. Glucose/GLU 1012 Glucose oxidase (GOD Trinder): Glucose oxidase catalyzes the oxidation of glucose by forming gluconic acid and hydrogen peroxide. The formed hydrogen peroxide reacts with 4-aminoantipyrine and phenol under peroxidase catalyzing action through an oxidative coupling reaction to form a red antipyrilquinonimine whose color intensity is proportional to the glucose concentration in the sample Lactate dehydrogenase/LDH 86 UV piruvate to lactate: LDH catalyzes the conversion of pyruvate into lactate in the presence of NADH. The drop-in absorbance at 340nm due to NADH oxidation is proportional to the LDH activity in the sample Total protein/TP 99 Biuret: Copper ions (Cu2 +) in the alkaline medium (Biuret Reactant) react with the peptide bonds of the serum proteins to form a purple color, which has a maximum absorbance at 545nm that is proportional to the concentration of the proteins in the sample. Uric acid/UA 140-1Q Uricase-peroxidase: Uric acid is oxidized by uricase to allantoin and hydrogen peroxide. Hydrogen peroxide in the presence of peroxidase reacts with DHBS and 4-aminoantipyrine to form the chromogen antipyrilquinonimine. The intensity of the red color formed is directly proportional to the uric acid concentration in the sample. Urea/BUN 104-2b UV enzyme: urease-GLDH: Urea is hydrolyzed by urease to produce ammonia and carbon dioxide. Ammonia reacts with 2-ketoglutarate and NADH in a reaction catalyzed by glutamate dehydrogenase (GLDH) by promoting the oxidation of NADH to NAD. The resulting drop in absorbance measured at 340nm is proportional to the urea concentration in the sample. Triglycerides/TG 87-2P Glycerolperoxidase: Lipoprotein lipase promotes the hydrolysis of triglycerides by releasing glycerol, which is converted by glycerol kinase into glycerol-3-phosphate. This is oxidized to dihydroxyacetone and hydrogen peroxide in the presence of glycerol phosphate oxidase. Then a coupling reaction occurs between hydrogen peroxide, 4-aminoantipyrine and 4-chlorophenol that is catalyzed by peroxidase to produce a quinoneimine with a maximum absorbance at 505nm. The intensity of the formed red color is directly proportional to the concentration of the triglycerides in the sample.
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