PubMed · 14332483
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L S KAPLOW. 1965. SIMPLIFIED MYELOPEROXIDASE STAIN USING BENZIDINE DIHYDROCHLORIDE.. https://pubmed.ncbi.nlm.nih.gov/14332483/
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The rapid interaction between o-tolidine and p-toluidine (pi-donors) with the pi-acceptors, e.g., 3,5-dinitrobenzoic acid (DNB) and 2,6-dichloroquinone-4-chloroimide (DCQ) results in the formation of 1:1 charge-transfer complexes as the final products, [(o-tolidine) (acceptor)] and [(p-toluidine) (acceptor)]. The final products of the reactions have been isolated and characterized using FTIR, 1HNMR spectroscopy and elemental analysis as well as photometric titration. The stoichiometry and apparent formation constants of the complexes formed were determined by applying the conventional spectrophotometric molar ratio method.
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We describe a new assay for the chlorination activity of myeloperoxidase and detection of chloramines. Chloramines were detected by using iodide to catalyze the oxidation of either 3,3',5,5'-tetramethylbenzidine (TMB) or dihydrorhodamine to form strongly absorbing or fluorescent products, respectively. With TMB as little as 1 muM taurine chloramine could be detected. The sensitivity of the dihydrorhodamine assay was about 10-fold greater. The chlorination activity of myeloperoxidase was measured by trapping hypochlorous acid with taurine and subsequently using iodide to promote the oxidation reactions of the accumulated taurine chloramine. A similar approach was used to detect hypochlorous acid production by stimulated human neutrophils. Iodide-dependent catalysis distinguished N-chloramines from N-bromamines. This allows for discrimination between heme peroxidases that generate either hypochlorous acid or hypobromous acid. The assay has distinct advantages over existing assays for myeloperoxidase with regard to sensitivity, specificity, and its ease and versatility of use.