Cromatest

Gamma-glutamyltransferase (g-GT) catalyses the transfer of the g-glutamyl group from g-glutamyl-3-carboxy-4-nitroanilide to glycylglyclycine with the formation of L-g-glutamyl- glycylglycine and 5-amino-2-nitrobenzoate. The amount of 5-amino-2-nitrobenzoate formed, kinetically monitored at 405 nm, is proportional to the g-GT activity present in the sample.

Gamma-glutamyltransferase (g-GT) catalyses the transfer of the g-glutamyl group from g-glutamyl-3-carboxy-4-nitroanilide to glycylglyclycine with the formation of L-g-glutamyl- glycylglycine and 5-amino-2-nitrobenzoate. The amount of 5-amino-2-nitrobenzoate formed, kinetically monitored at 405 nm, is proportional to the g-GT activity present in the sample.

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.

The method is based on the specific binding of arsenazo III and calcium at an acidic pH, resulting in a shift in the absorption spectrum of the complex. The intensity of the formed chromophore is proportional to the total calcium concentration in the sample.

The method is based on the specific binding of arsenazo III and calcium at an acidic pH, resulting in a shift in the absorption spectrum of the complex. The intensity of the formed chromophore is proportional to the total calcium concentration in the sample.

The method is based on the specific binding of arsenazo III and calcium at an acidic pH, resulting in a shift in the absorption spectrum of the complex. The intensity of the formed chromophore is proportional to the total calcium concentration in the sample.

The method is based on the specific binding of cresolphtalein complexone (OCC), a metalochromic indicator, and calcium at an alkaline pH, resulting in a shift in the absorption spectrum.

Chloride ions in the sample quantitatively displace thiocyanate ions from their mercuric salt. The free thiocyanate reacts with ferric ions, forming a complex proportional to the concentration of chlorides present in the sample.

Chloride ions in the sample quantitatively displace thiocyanate ions from their mercuric salt. The free thiocyanate reacts with ferric ions, forming a complex proportional to the concentration of chlorides present in the sample.

Chloride ions in the sample quantitatively displace thiocyanate ions from their mercuric salt. The free thiocyanate reacts with ferric ions, forming a complex proportional to the concentration of chlorides present in the sample.

This method for the determination of total cholesterol in serum is based on the use of three enzymes: cholesterol esterase (CE), cholesterol oxidase (CO), and peroxidase (POD). In the presence of the latter, the mixture of phenol and 4-aminoantipyrine (4-AA) condenses due to hydrogen peroxide, forming a colored quinonimine proportional to the concentration of cholesterol in the sample.

This method for the determination of total cholesterol in serum is based on the use of three enzymes: cholesterol esterase (CE), cholesterol oxidase (CO), and peroxidase (POD). In the presence of the latter, the mixture of phenol and 4-aminoantipyrine (4-AA) condenses due to hydrogen peroxide, forming a colored quinonimine proportional to the concentration of cholesterol in the sample.