Clonatest

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

Inorganic phosphate reacts with molybdic acid to form a phosphomolybdic complex. The subsequent reduction of the complex in an alkaline medium produces a blue molybdenum color whose intensity is proportional to the amount of phosphorus present in the sample.

This technique employs a separation method based on the selective precipitation of apoprotein-B-containing lipoproteins (VLDL, LDL and (a)Lpa) by the action of phosphotungstic acid/Cl2Mg, sedimentation of the precipitate by centrifugation and subsequent enzymatic analysis as residual cholesterol from the high-density lipoproteins (HDL) contained in the clear supernatant.

The Fe(II) of all forms of haemoglobin, with the exception of sulphohaemoglobin, is oxidised by ferrocyanide to Fe(III) to methaemoglobin, which in turn reacts with ionised cyanide (CN-) to form cyanmethaemoglobin, a very stable derivative that absorbs at 540 nm. The intensity of the colour formed is proportional to the concentration of total haemoglobin in the sample.

The Fe3+ transported by serum transferrin, once dissociated in a slightly acid medium by the action of Teepol and guanidinium chloride, is reduced by the action of hydroxylamine to Fe2+, forming the ferrous ion in the presence of FerroZine a coloured complex proportional to the concentration of iron present in the sample.

Lactate dehydrogenase (LDH/LD) catalyzes the reduction of pyruvate to lactate (P-L) in the presence of reduced nicotinamide adenine dinucleotide (NADH) at pH 7.5. The reaction is kinetically controlled at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+

The Fe3+ transported by serum transferrin, once dissociated in a slightly acid medium by the action of Teepol and guanidinium chloride, is reduced by the action of hydroxylamine to Fe2+, forming the ferrous ion in the presence of FerroZine a coloured complex proportional to the concentration of iron present in the sample.

In the Trinder reaction, glucose is oxidised to D-gluconate by glucose oxidase (GOD), with formation of hydrogen peroxide. In the presence of peroxidase (POD), phenol and 4-aminoantipyrine (4-AA) are condensed by hydrogen peroxide, forming a red quinoneimine proportional to the concentration of glucose 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.

In the Trinder reaction, glucose is oxidised to D-gluconate by glucose oxidase (GOD), with formation of hydrogen peroxide. In the presence of peroxidase (POD), phenol and 4-aminoantipyrine (4-AA) are condensed by hydrogen peroxide, forming a red quinoneimine proportional to the concentration of glucose in the sample.

This technique employs a separation method based on the selective precipitation of apoprotein-B-containing lipoproteins (VLDL, LDL and (a)Lpa) by the action of phosphotungstic acid/Cl2Mg, sedimentation of the precipitate by centrifugation and subsequent enzymatic analysis as residual cholesterol from the high-density lipoproteins (HDL) contained in the clear supernatant.

In the Trinder reaction, glucose is oxidised to D-gluconate by glucose oxidase (GOD), with formation of hydrogen peroxide. In the presence of peroxidase (POD), phenol and 4-aminoantipyrine (4-AA) are condensed by hydrogen peroxide, forming a red quinoneimine proportional to the concentration of glucose in the sample.