Interruption of the MnO2 oxidative process on dopamine and L-dopa by the action of S2O3(2-).

The oxidation effects of Mn2+, Mn3+ or MnO2 on dopamine can be studied in vitro and, therefore, this offers a model of the auto-oxidation process that appears naturally in neurons causing Parkinson's disease. The use of MnO, as an oxidizer in aqueous solution at pH 7 causes the oxidation of catecholamines (L-dopa, dopamine, noradrenaline and adrenaline) to melanin. However, this work shows that, in water at pH 6-7, the oxidation of catecholamines by MnO2 in the presence of sodium thiosulphate (Na2S2O3) occurs by other mechanisms. For dopamine and L-dopa, MLCT complexes were formed with bands at 312, 350 (sh), 554 (sh) nm, and an intense band at 597 nm (epsilon approximately/= 4 x 10(3) M(-1) cm(-1)) and at ca. 336, 557 (sh) nm, and an intense band at 597 nm (epsilon approximately 6 x 10(3) M(-1) cm(-1)), respectively. The latter transitions were assigned to d(pi)-->pi*-SQ. Noradrenaline and adrenaline do not form this blue complex in solution, but generate soluble oxidized compounds. The resonance Raman spectra of these complexes in solution showed bands at 950, 1006, 1258, 1378, 1508 and 1603 cm(-1) for the complex derivation of L-dopa and at 948, 1010, 1255, 1373, 1510 and 1603 cm(-1) for the dopamine-derived compound. The most intense Raman band at ca. 1378 cm(-1) was assigned to C-O stretching with major C1-C2 characteristics and indicated that dopamine and L-dopa do not occur complexed with manganese in the catecholate or quinone form, but suggests an intermediate compound such as an anionic o-semiquinone (SQ-), forming a complex such as [Mn(II)(SQ-)3]-. All enhanced Raman frequencies are characteristic of the benzenic ring without the participation of the aminic nitrogen. A mechanism is proposed for the formation of the dopamine and L-dopa complexes and a computational simulation was performed to support it.

Spectrophotometric determination of total proteins in blood plasma with p-benzoquinone.

1. In the present study we have documented the use of the reagent, p-benzoquinone (PBQ) for the spectrophotometric determination of total proteins in blood plasma. 2. Since the products of reaction are stable for several hours at room temperature after the 20-min boiling step, the time at which absorbance is measured is not a critical factor. 3. Common anticoagulants such as EDTA, citrate, or heparin do not interfere with the PBQ method at concentrations used in clinical laboratories. 4. The products of the reaction between PBQ and either plasma (specific absorbance 2.33 x 10(-3) +/- 0.20 x 10(-3) micrograms cm-2) or purified proteins (specific absorbance 2.61 x 10(-3) +/- 0.31 x 10(-3) micrograms cm-2) show an absorption band at 350 nm, which follows Beer's law, and therefore can be used for analytical purposes. 5. The PBQ method has a lower limit of detection (4 micrograms/ml) than that of the biuret method (45 micrograms/ml) for a final reaction mixture of 5.0 and 4.2 ml, respectively.

Spectrophotometric determination of total proteins in blood plasma with p-benzoquinone

In the present study we have documented the use of the reagent p-benzoquinone (PBQ) for the spectrophotometric determination of total protein in blood plasma. Since the products of reaction are stable for several hours at room temperature after the 20-min boiling step, the time at which absorbance is measured is not a critical factor. Common anticoagulants such as EDTYA, citrate, or heparin do not interfere with the PBQ method at concentrations used in clinical laboratories. The products of the reaction between PBQ and either plasma (specific absorbance 2.33 x 10-3 ñ 0.20 x 10-3 ug cm -2) or purified proteins (specific absorbance 2.61 x 10-3 ñ 0.31 x 10-3 ug cm-2) show an absorption band at 350 nm, which follows Beer's law, and therefore can be used for analytical purposes. The PBQ method has a lower limit of detection (4 ug/ml) than that of biuret method (45 yg/ml) for a final reaction mixture of 5.0 and 4.2 ml, respectively