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Chemical Compound Review

Dianisidine     4-(4-amino-3-methoxy-phenyl)- 2-methoxy...

Synonyms: o-Dianisidin, o-Dianisidina, o-Dianisidine, Cellitazol B, Cellitazol bn, ...
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Disease relevance of Dianisidine


Psychiatry related information on Dianisidine

  • The enzymic oxidation determined colorimetrically by transferring the peroxide formed to o-dianisidine ceased at a maximum typical for each substrate and independent of the reaction time [6].

High impact information on Dianisidine

  • Our data show that this enzyme has a striking biochemical similarity to mammalian myeloperoxidase (MPO; EC 1.11.17), an antimicrobial dianisidine peroxidase that occurs in neutrophils [7].
  • The peroxidation of dianisidine catalyzed by cytochrome c peroxidase was affected by the nitrogenous compounds, but to a lesser extent than was the action of HRP [8].
  • 5. The enzyme differs from typical catalases in also having a strong peroxidatic activity with dianisidine, pyrogallol, and diaminobenzidine as electron donors [9].
  • Molar consumption of NADPH and O(2) and molar H(2)O(2) production (o-dianisidine oxidation) revealed that Group 1 compounds mostly increased, Group 2 had no effect, and Group 3 decreased the H(2)O(2)/O(2) and H(2)O(2)/NADPH ratios [10].
  • Dianisidine- and nonspecific esterase-positive TER-3 cells increase with granulocyte-colony stimulating factor (G-CSF) rather than with IL-3 [11].

Chemical compound and disease context of Dianisidine

  • In 115 patients with chronic lymphocytic leukemia (CLL), grouped according to the staging system as proposed by Rai et al., dipeptidylpeptidase II (DPP II) reaction was carried out in smears of peripheral blood using Lys-Pro-MNA and Lys-Ala-MNA as substrates and Fast Blue B (FBB) as the coupling agent in cacodylate buffer, pH 5 [12].

Biological context of Dianisidine


Anatomical context of Dianisidine

  • Infected corneas were examined immunohistochemically for infiltrating leukocytes and assayed for myeloperoxidase activity using the dye o-dianisidine [18].
  • DCB was the most activated of the benzidines, with activation by the 3 systems being in the order: S9 = S9-Ac greater than microsomes, whereas dianisidine and tolidine were the least activated [19].
  • 5. We focused our attention on chronic plaques, recognized by the absence of Luxol Fast Blue B-positive inclusions in macrophages [20].
  • D-Val-Leu-Arg-4-methoxy-2-naphthylamide (MNA) plus Fast Blue B was the best for identifying human mast cells, yielding the most specific and complete staining [21].
  • Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide [22].

Associations of Dianisidine with other chemical compounds

  • The PE activity bands on polyacrylamide gels after native acidic PAGE or SDS-PAGE were stained with a combination of tetrazotized o-dianisidine and beta-NA [23].
  • During the course of horseradish peroxidase-mediated oxidation of either o-dianisidine or 2-2'-azino-di(3-ethyl-benzthiazoline-6-sulfonic acid) (ABTS), no O2 consumption took place [24].
  • The phrenic nucleus of the adult albino rat was studied by utilizing the O-dianisidine method for the retrograde transport of horseradish peroxidase in conjunction with the zinc chromate modification of the Golgi technique [25].
  • We compared the abilities of recombinant MnPs to use various substrates and found that rH4 could oxidize o-dianisidine and p-anisidine without externally added manganese, a property not previously reported for this MnP isoenzyme from P. chrysosporium [26].
  • The mechanism of myoglobin/H2O2 derived peroxidation of myosin was studied by comparing the catalytic activity of myoglobin and horseradish peroxidase using O-dianisidine, N-acetyl tyrosine and myosin as substrates [27].

Gene context of Dianisidine

  • An assay was developed using o-dianisidine as the electron donor which considerably reduced the interference by EPO [28].
  • Enzyme immunoassay was found to be clearly more sensitive than o-dianisidine or o-tolidine in detecting HP bands from diluted serum samples [29].
  • Erythroid differentiation of F55 cells, which was characterized by an increase in dianisidine-positive cells, was also induced by activin A/EDF [30].
  • The selectivity of both amperometric measurements was demonstrated through the use of known hydrogen peroxide scavengers (added catalase or intracellular peroxidase + added o-dianisidine) to the media bathing the cells [31].
  • The recombinant enzyme showed the same ratio of catalase activity to peroxidase activity with o-dianisidine and the same Km for H2O2 as the native enzyme [32].

Analytical, diagnostic and therapeutic context of Dianisidine


  1. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. Claiborne, A., Fridovich, I. J. Biol. Chem. (1979) [Pubmed]
  2. Qualitative detection of selenium in fortified soil and water samples by a paper chromatographic-carboxyl esterase enzyme inhibition technique. Saritha, K., Nanda Kumar, N.V. Journal of chromatography. A. (2001) [Pubmed]
  3. Fast blue salt B can detect phenylketonuria and tyrosinaemia in addition to methylmalonic acidaemia. Schlesinger, P., Grimes, A., Hammond, J. Clin. Chim. Acta (1979) [Pubmed]
  4. Mutagenicity of some benzidine congeners and their N-acetylated and N,N'-diacetylated derivatives in different strains of Salmonella typhimurium. Reid, T.M., Wang, C.Y., King, C.M., Morton, K.C. Environmental mutagenesis. (1984) [Pubmed]
  5. Improved myeloperoxidase assay for quantitation of neutrophil influx in a rat model of endotoxin-induced uveitis. Graff, G., Gamache, D.A., Brady, M.T., Spellman, J.M., Yanni, J.M. Journal of pharmacological and toxicological methods. (1998) [Pubmed]
  6. The reactivity of galactose oxidase with snail galactans, galactosides and D-galactose-composed oligosaccharides. Bretting, H., Jacobs, G. Biochim. Biophys. Acta (1987) [Pubmed]
  7. A peroxidase related to the mammalian antimicrobial protein myeloperoxidase in the Euprymna-Vibrio mutualism. Weis, V.M., Small, A.L., McFall-Ngai, M.J. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  8. Stimulation of the activity of horseradish peroxidase by nitrogenous compounds. Kuo, C.F., Fridovich, I. J. Biol. Chem. (1988) [Pubmed]
  9. Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata. Hochman, A., Shemesh, A. J. Biol. Chem. (1987) [Pubmed]
  10. Uncoupling-mediated generation of reactive oxygen by halogenated aromatic hydrocarbons in mouse liver microsomes. Shertzer, H.G., Clay, C.D., Genter, M.B., Chames, M.C., Schneider, S.N., Oakley, G.G., Nebert, D.W., Dalton, T.P. Free Radic. Biol. Med. (2004) [Pubmed]
  11. New human myelodysplastic cell line, TER-3: G-CSF specific downregulation of Ca2+/calmodulin-dependent protein kinase IV. Mishima, Y., Terui, Y., Mishima, Y., Katsuyama, M., Mori, M., Tomizuka, H., Takizawa, T., Miyazato, A., Ueda, M., Yamada, M., Hayasawa, H., Mizunuma, N., Ishizaka, Y., Ikeda, K., Kato, T., Ozawa, K., Hatake, K. J. Cell. Physiol. (2002) [Pubmed]
  12. Possible prognostic significance of the assessment of dipeptidylpeptidase II in peripheral blood lymphocytes of patients with chronic lymphocytic leukemia. Klener, P., Lojda, Z., Háber, J., Kvasnicka, J. Neoplasma (1987) [Pubmed]
  13. DNA damage induced by 3,3'-dimethoxybenzidine in liver and urinary bladder cells of rats and humans. Martelli, A., Robbiano, L., Carrozzino, R., Puglia, C.P., Mattioli, F., Angiola, M., Brambilla, G. Toxicol. Sci. (2000) [Pubmed]
  14. Erythropoiesis in the developing rainbow trout, Salmo gairdneri irideus: histochemical and immunochemical detection of erythropoietic organs. Iuchi, I., Yamamoto, M. J. Exp. Zool. (1983) [Pubmed]
  15. Investigations into the cellular contribution to host tissue proteases and inhibitors in gingival crevicular fluid. Kennett, C.N., Cox, S.W., Eley, B.M. Journal of clinical periodontology. (1997) [Pubmed]
  16. NADPH-dependent lipid peroxidation capacity in unfixed tissue sections: characterization of the pro-oxidizing conditions and optimization of the histochemical detection. Thomas, M., Frederiks, W.M., Van Noorden, C.J., Bosch, K.S., Pompella, A. Histochem. J. (1994) [Pubmed]
  17. A continuous spectrophotometric assay for the determination of diamondback moth esterase activity. He, X. Arch. Insect Biochem. Physiol. (2003) [Pubmed]
  18. Role of MIP-2 in neutrophil migration and tissue injury in the herpes simplex virus-1-infected cornea. Yan, X.T., Tumpey, T.M., Kunkel, S.L., Oakes, J.E., Lausch, R.N. Invest. Ophthalmol. Vis. Sci. (1998) [Pubmed]
  19. Comparative activation of 3,3'-dichlorobenzidine and related benzidines to mutagens in the Salmonella typhimurium assay by hepatic S9 and microsomes from rats pretreated with different inducers of cytochrome P-450. Iba, M.M. Mutat. Res. (1987) [Pubmed]
  20. Abnormal ubiquitination of axons in normally myelinated white matter in multiple sclerosis brain. Giordana, M.T., Richiardi, P., Trevisan, E., Boghi, A., Palmucci, L. Neuropathol. Appl. Neurobiol. (2002) [Pubmed]
  21. Selection of a simple protease procedure for identifying mast cells in routinely processed human tissues. Garrett, J.R., Osman, I.A., Smith, R.E. J. Histochem. Cytochem. (1987) [Pubmed]
  22. The salivary catechol oxidase/peroxidase activities of the mosquito Anopheles albimanus. Ribeiro, J.M., Nussenzveig, R.H. J. Exp. Biol. (1993) [Pubmed]
  23. Activity staining of pectinesterase on polyacrylamide gels after acidic or sodium dodecyl sulfate electrophoresis. Hou, W.C., Lin, Y.H. Electrophoresis (1998) [Pubmed]
  24. Enzymatic and nonenzymatic superoxide-generating reactions of isoniazid. Shoeb, H.A., Bowman, B.U., Ottolenghi, A.C., Merola, A.J. Antimicrob. Agents Chemother. (1985) [Pubmed]
  25. The phrenic nucleus of th albino rat: a correlative HRP and Golgi study. Goshgarian, H.G., Rafols, J.A. J. Comp. Neurol. (1981) [Pubmed]
  26. Isoenzyme multiplicity and characterization of recombinant manganese peroxidases from Ceriporiopsis subvermispora and Phanerochaete chrysosporium. Larrondo, L.F., Lobos, S., Stewart, P., Cullen, D., Vicuña, R. Appl. Environ. Microbiol. (2001) [Pubmed]
  27. The role of H2O2-generated myoglobin radical in crosslinking of myosin. Hanan, T., Shaklai, N. Free Radic. Res. (1995) [Pubmed]
  28. Incidence of myeloperoxidase deficiency in an area of northern Italy: histochemical, biochemical and functional studies. Cramer, R., Soranzo, M.R., Dri, P., Rottini, G.D., Bramezza, M., Cirielli, S., Patriarca, P. Br. J. Haematol. (1982) [Pubmed]
  29. Haptoglobin phenotyping from older bloodstains by enzyme immunoassay and haptoglobin phenotypes within a Nebraska Caucasian population. Roy, R., Roy, I.C. J. Forensic Sci. (1991) [Pubmed]
  30. Effects of activin A/erythroid differentiation factor on erythroid and megakaryocytic differentiations of mouse erythroleukemia (Friend) cells: evidence for two distinct modes of cell response. Okafuji, K., Kaku, K., Seguchi, M., Tanaka, H., Azuno, Y., Kaneko, T. Exp. Hematol. (1995) [Pubmed]
  31. Monitoring an oxidative stress mechanism at a single human fibroblast. Arbault, S., Pantano, P., Jankowski, J.A., Vuillaume, M., Amatore, C. Anal. Chem. (1995) [Pubmed]
  32. The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli. Mutsuda, M., Ishikawa, T., Takeda, T., Shigeoka, S. Biochem. J. (1996) [Pubmed]
  33. Cannabis sativa L. (Marijuana). VII. The relative specificity of the RIM test. Segelman, A.B., Segelman, F.P. J. Chromatogr. (1976) [Pubmed]
  34. C-terminal truncation of WT1 delays but does not abolish hematopoiesis in embryoid bodies. Wagner, K.J., Patek, C.E., Cunningham, A., Taylor, A.H., Hooper, M.L., Ansell, J.D. Blood Cells Mol. Dis. (2002) [Pubmed]
  35. Observations on the staining of ceruloplasmin following disc-electrophoresis utilizing polyacrylamide gels. Macbeth, R.A., Bazin, S., Allain, J.C. Clin. Biochem. (1975) [Pubmed]
  36. Comparison of chromogens for the determination of horseradish peroxidase as a marker in enzyme immunoassay. Porstmann, B., Porstmann, T., Nugel, E. J. Clin. Chem. Clin. Biochem. (1981) [Pubmed]
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