Clonatest

The method is based on the enzymatic hydrolysis of serum triglycerides to glycerol and free fatty acids (FFA) by the action of lipoprotein lipase (LPL). Glycerol is phosphorylated by adenosine triphosphate (ATP) in the presence of glycerol kinase (GK) to form glycerol-3-phosphate (G-3-P) and adenosine diphosphate (ADP). G-3-P is oxidized by glycerophosphate oxidase (GPO) to dihydroxyacetone phosphate (DHAP) and hydrogen peroxide. In the presence of peroxidase (POD)

En la reacción del biuret se forma un quelato entre el ión Cu2+ y los enlaces peptídicos de las proteínas en medio alcalino con la formación de un complejo coloreado violeta cuya absorbancia se mide fotométricamente. La intensidad del color producido es proporcional a la concentración de proteínas en la muestra.

En la reacción del biuret se forma un quelato entre el ión Cu2+ y los enlaces peptídicos de las proteínas en medio alcalino con la formación de un complejo coloreado violeta cuya absorbancia se mide fotométricamente. La intensidad del color producido es proporcional a la concentración de proteínas en la muestra.

Serum iron is bound to transferrin, but only one third of its capacity is saturated. The unsaturated binding capacity of transferrin or residual binding capacity (RBC) is indicative of the availability of serum binding receptors. The amount of iron that serum transferrin can bind when fully saturated with excess Fe3+ is the total binding capacity (TFC). The method measures the TFC by first saturating the transferrin with excess Fe3+. The excess iron is adsorbed with magnesium carbonate and once the binding process is complete, it is removed by centrifugation and the iron in the supernatant is determined. The figure found corresponds to the CFT. When the determination of serum iron is carried out at the same time as the TFR and the result is subtracted from the TFR value, the difference gives the free binding capacity (FBC), or serum transferrin not bound to iron.

Reagent for the in vitro quantitative determination of sodium in human serum for the control of electrolyte balance in the diagnosis and treatment of diseases characterized by high or low blood sodium levels. Sodium is determined through the sodium-dependent b-galactosidase enzymatic activity with ONPG as a substrate. The absorbance at 405 nm of the O-nitrophenyl product is proportional to the sodium concentration.

The method measures the shift of the maximum absorption peak from 460 to 600 nm of the complex formed at acidic pH between red pyrogallol-molybdate (RPM) and the basic amino groups of urine and cerebrospinal fluid (CSF) proteins. The intensity of the formed colored complex is proportional to the protein concentration in the sample.

Reagent for the in vitro quantitative determination of potassium in human serum for the control of electrolyte balance in the diagnosis and treatment of diseases characterized by high or low blood potassium levels. Potassium is determined spectrophotometrically by kinetic assay using potassium-dependent pyruvate kinase. The generated pyruvate is converted into lactate present in the conversion of NADH to NAD. The corresponding decrease in optical density at 380 nm is proportional to the potassium concentration in the serum.

Reagent for the in vitro quantitative determination of potassium in human serum for the control of electrolyte balance in the diagnosis and treatment of diseases characterized by high or low blood potassium levels. Potassium is determined spectrophotometrically by kinetic assay using potassium-dependent pyruvate kinase. The generated pyruvate is converted into lactate present in the conversion of NADH to NAD. The corresponding decrease in optical density at 380 nm is proportional to the potassium concentration in the serum.

Inorganic phosphate reacts with ammonium molybdate in an acidic medium to form a phosphomolybdic complex measured at 340 nm.

The method is based on the specific binding of calmagite, a metallochromic indicator, to magnesium at alkaline pH with a consequent shift of the absorption spectrum of the complex. The intensity of the chromophore formed is proportional to the concentration of magnesium present in the sample.

The method is based on the segmentation of the specific chromogenic substrate 1,2-O-dilaurylrac-glycero-3-glutaric- (6'methyl-resorufin)-ester emulsified in stabilising micro-particles. In the presence of specific pancreatic lipase activators such as colipase, calcium ions and bile acids, the substrate is transformed into 1,2-O-dilauryl-rac-glycerol and glutaric acid-6′-methylresorufinester which spontaneously decomposes to glutaric acid and methylresorufin. The intensity of the colour formed is proportional to the concentration of lipase in the sample.

This technique employs a separation method based on the specific precipitation of low density lipoproteins (LDL) by polyvinyl sulphate in serum, sedimentation of the precipitate by centrifugation and subsequent assay as residual cholesterol of the remaining lipoproteins (HDL + VLDL) contained in the clear supernatant. LDL-cholesterol is calculated by difference, subtracting the supernatant cholesterol from the total cholesterol in the sample.