Cromatest

Diazotized sulfanilic acid transforms bilirubin into colored azobilirubin, which is determined photometrically. Of the two fractions of bilirubin present in serum, bilirubin glucuronate and bilirubin free associated with albumin, only the first reacts directly, while the free bilirubin needs to be dissociated from the protein by an accelerator to react. Indirect bilirubin is calculated by the difference between total bilirubin (with accelerator) and direct bilirubin (without accelerator). The concepts of 'direct' and 'indirect' refer exclusively to the reaction characteristics in the presence or absence of accelerators or solubilizers and are only approximate equivalents to the two mentioned bilirubin fractions.

Diazotized sulfanilic acid transforms bilirubin into colored azobilirubin, which is determined photometrically. Of the two fractions of bilirubin present in serum, bilirubin glucuronate and bilirubin free associated with albumin, only the first reacts directly, while the free bilirubin needs to be dissociated from the protein by an accelerator to react. Indirect bilirubin is calculated by the difference between total bilirubin (with accelerator) and direct bilirubin (without accelerator). The concepts of 'direct' and 'indirect' refer exclusively to the reaction characteristics in the presence or absence of accelerators or solubilizers and are only approximate equivalents to the two mentioned bilirubin fractions.

Diazotized sulfanilic acid transforms bilirubin into colored azobilirubin, which is determined photometrically. Of the two fractions of bilirubin present in serum, bilirubin glucuronate and bilirubin free associated with albumin, only the first reacts directly, while the free bilirubin needs to be dissociated from the protein by an accelerator to react. Indirect bilirubin is calculated by the difference between total bilirubin (with accelerator) and direct bilirubin (without accelerator). The concepts of 'direct' and 'indirect' refer exclusively to the reaction characteristics in the presence or absence of accelerators or solubilizers and are only approximate equivalents to the two mentioned bilirubin fractions.

Diazotized sulfanilic acid transforms bilirubin into colored azobilirubin, which is determined photometrically. Of the two fractions of bilirubin present in serum, bilirubin glucuronate and bilirubin free associated with albumin, only the first reacts directly, while the free bilirubin needs to be dissociated from the protein by an accelerator to react. Indirect bilirubin is calculated by the difference between total bilirubin (with accelerator) and direct bilirubin (without accelerator). The concepts of 'direct' and 'indirect' refer exclusively to the reaction characteristics in the presence or absence of accelerators or solubilizers and are only approximate equivalents to the two mentioned bilirubin fractions.

Direct (conjugated) bilirubin reacts with the diazonium salt 2,4-dichlorophenyldiazonium (2,4-DPD) in the presence of sulfamic acid, forming azobilirubin. This colored complex can be measured photometrically at 546 nm. Of the two fractions of bilirubin present in serum, bilirubin glucuronate (conjugated) and bilirubin free associated with albumin (unconjugated), only the first reacts directly, while the free bilirubin needs to be dissociated from the protein by an accelerator to react. Indirect bilirubin is calculated by the difference between total bilirubin (with accelerator) and direct bilirubin (without accelerator). The concepts of 'direct' and 'indirect' refer exclusively to the reaction characteristics in the presence or absence of accelerators or solubilizers and are only approximate equivalents to the two mentioned bilirubin fractions.

Alkaline phosphatases (FAL) catalyze the hydrolysis of 4-nitrophenyl phosphate (4-NFF) to form 4-nitrophenol and inorganic phosphate, with the alkaline buffer acting as a phosphate acceptor. The reaction is kinetically monitored at 405 nm based on the rate of 4-nitrophenol formation, proportional to the FAL activity present in the sample.

Alkaline phosphatases (FAL) catalyze the hydrolysis of 4-nitrophenyl phosphate (4-NFF) to form 4-nitrophenol and inorganic phosphate, with the alkaline buffer acting as a phosphate acceptor. The reaction is kinetically monitored at 405 nm based on the rate of 4-nitrophenol formation, proportional to the FAL activity present in the sample.

Alanine aminotransferase (ALT/GPT) catalyzes the transfer of the amino group from alanine to alpha-ketoglutarate, forming glutamate and pyruvate. The latter is reduced to lactate by lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

Alanine aminotransferase (ALT/GPT) catalyzes the transfer of the amino group from alanine to alpha-ketoglutarate, forming glutamate and pyruvate. The latter is reduced to lactate by lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

Alanine aminotransferase (ALT/GPT) catalyzes the transfer of the amino group from alanine to alpha-ketoglutarate, forming glutamate and pyruvate. The latter is reduced to lactate by lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

Alanine aminotransferase (ALT/GPT) catalyzes the transfer of the amino group from alanine to alpha-ketoglutarate, forming glutamate and pyruvate. The latter is reduced to lactate by lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

Lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm through the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.