Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10557387 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2005 | 4 Pages |
Abstract
A new method has been developed for the determination of myoglobin (Mb) based on its enzymatic activity for the oxidation of o-phenylenediamine (OPDA) with hydrogen peroxide. Stopped-flow spectrophotometry was used to study the kinetic behavior of the oxidation reaction. The catalytic activity of Mb was compared to other three kinds of catalyst. The time dependent absorbance of the reaction product, 2,3-diamimophenazine (DAPN), at a wavelength of 426 nm was recorded. The initial reaction rate obtained at 40 °C was found to be proportional to the concentration of Mb in the range of 1.0 à 10â6 to 4.0 à 10â9 mol Lâ1. The detection limit of Mb was found to be 9.93 à 10â10 mol Lâ1. The relative standard deviations were within 5% for the determination of different concentrations of Mb. Excess of bovine serum albumin (BSA), Ca(II), Mg(II), Cu(II), glucose, caffeine, lactose and uric acid did not interfere.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Qi Zheng, Zhihong Liu, Ruxiu Cai,