Cromatest

The higher activity of CK in normal sera is due to the isoenzymes CK-MM and CK-MB present in muscle and cardiac tissues. CK-BB is usually present at very low concentrations. Both creatine kinase (CK) enzymes are dimers formed by the association of two muscle (M) and brain (B) subunits. Immunoinhibition with a specific antibody for both MM subunits and the individual unit of CK-MB allows the determination of the B subunit. The activity corresponding to half of CK-MB is measured through the increase in absorbance resulting from coupled reactions.

The higher activity of CK in normal sera is due to the isoenzymes CK-MM and CK-MB present in muscle and cardiac tissues. CK-BB is usually present at very low concentrations. Both creatine kinase (CK) enzymes are dimers formed by the association of two muscle (M) and brain (B) subunits. Immunoinhibition with a specific antibody for both MM subunits and the individual unit of CK-MB allows the determination of the B subunit. The activity corresponding to half of CK-MB is measured through the increase in absorbance resulting from coupled reactions.

This procedure is based on a modification of the original picrate (Jaffe) reaction. Creatinine, under alkaline conditions, reacts with picrate ions, forming a reddish complex. The rate of complex formation measured through the increase in absorbance over a predetermined time interval is proportional to the concentration of creatinine in the sample.

This procedure is based on a modification of the original picrate (Jaffe) reaction. Creatinine, under alkaline conditions, reacts with picrate ions, forming a reddish complex. The rate of complex formation measured through the increase in absorbance over a predetermined time interval is proportional to the concentration of creatinine in the sample.

This procedure is based on a modification of the original picrate (Jaffe) reaction. Creatinine, under alkaline conditions, reacts with picrate ions, forming a reddish complex. The rate of complex formation measured through the increase in absorbance over a predetermined time interval is proportional to the concentration of creatinine in the sample.

This procedure is based on a modification of the original picrate (Jaffe) reaction. Creatinine, under alkaline conditions, reacts with picrate ions, forming a reddish complex. The rate of complex formation measured through the increase in absorbance over a predetermined time interval is proportional to the concentration of creatinine in the sample.

This procedure is based on a modification of the original picrate (Jaffe) reaction. Creatinine, under alkaline conditions, reacts with picrate ions, forming a reddish complex. The rate of complex formation measured through the increase in absorbance over a predetermined time interval is proportional to the concentration of creatinine in the sample.

This procedure is based on a modification of the original picrate (Jaffe) reaction. Creatinine, under alkaline conditions, reacts with picrate ions, forming a reddish complex. The rate of complex formation measured through the increase in absorbance over a predetermined time interval is proportional to the concentration of creatinine in the sample.

This procedure is based on an improved enzymatic method originally designed to assess serum and urinary creatinine. The assay is performed in two stages. In the first stage, creatine is eliminated during the initial minutes of sample pre-incubation with creatinase. In the second stage, the addition of creatininase initiates the reaction, hydrolyzing creatinine in the sample in the presence of sarcosine oxidase (Sar OD) with the production of hydrogen peroxide:_x000D_ Creatinine + H2O → Creatine_x000D_ Sarcosine + H2O + O2 → H2O2 + Glycine + HCHO_x000D_ The hydrogen peroxide derived from the oxidase reaction is quantified by a Trinder-type reaction in which the chromogenic derivative HTIB and 4-aminoantipyrine (4-AA) condense in the presence of peroxidase (POD) to form a red quinonimine dye._x000D_ 4-AA + HTIB → Quinonimine + H2O_x000D_ The color development rate is proportional to the creatinine concentration in the sample.

This procedure is based on an improved enzymatic method originally designed to assess serum and urinary creatinine. The assay is performed in two stages. In the first stage, creatine is eliminated during the initial minutes of sample pre-incubation with creatinase. In the second stage, the addition of creatininase initiates the reaction, hydrolyzing creatinine in the sample in the presence of sarcosine oxidase (Sar OD) with the production of hydrogen peroxide:_x000D_ Creatinine + H2O → Creatine_x000D_ Sarcosine + H2O + O2 → H2O2 + Glycine + HCHO_x000D_ The hydrogen peroxide derived from the oxidase reaction is quantified by a Trinder-type reaction in which the chromogenic derivative HTIB and 4-aminoantipyrine (4-AA) condense in the presence of peroxidase (POD) to form a red quinonimine dye._x000D_ 4-AA + HTIB → Quinonimine + H2O_x000D_ The color development rate is proportional to the creatinine concentration in the sample.

This procedure is based on an improved enzymatic method originally designed to assess serum and urinary creatinine. The assay is performed in two stages. In the first stage, creatine is eliminated during the initial minutes of sample pre-incubation with creatinase. In the second stage, the addition of creatininase initiates the reaction, hydrolyzing creatinine in the sample in the presence of sarcosine oxidase (Sar OD) with the production of hydrogen peroxide:_x000D_ Creatinine + H2O → Creatine_x000D_ Sarcosine + H2O + O2 → H2O2 + Glycine + HCHO_x000D_ The hydrogen peroxide derived from the oxidase reaction is quantified by a Trinder-type reaction in which the chromogenic derivative HTIB and 4-aminoantipyrine (4-AA) condense in the presence of peroxidase (POD) to form a red quinonimine dye._x000D_ 4-AA + HTIB → Quinonimine + H2O_x000D_ The color development rate is proportional to the creatinine concentration 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.