Cromatest

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.

El método está basado en las propiedades del Cromazurol S (CAS), colorante cromogènico con alta afinidad para los iones Fe3+/Fe2+ que en condiciones ácidas en presencia de cetrimida (CTAB) forma un intenso complejo púrpura proporcional a la concentración de hierro presente en la muestra.

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.

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.

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+

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.

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.

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.

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.

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.