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DAB on Human Hepatocytes

Published online by Cambridge University Press:  14 March 2018

Charles S. Gilbert
Charles S. Gilbert*
Affiliation:
Carolinas Medical Center

Extract

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Neutrophil myeioperoxidase standard 3,3'-Diaminobenzidine Tetrahydrochioride (DAB) procedure:

When staining neutrophils, a cell suspension would be preferred, but a finely minced buffy coat can be used, if you thick section and locate the stained cells before thin sectioning. Staining should be carried out as soon as possible after fixation, The myeioperoxidase (MPO) activity falls off such that we process samples within 2-3 weeks of fixation.

Note that fixation is for 1 hour. Enzyme activity may be destroyed if tixed for longer periods.

Type
Research Article
Information
Microscopy Today , Volume 6 , Issue 2 , March 1998 , pp. 20 - 21
Copyright
Copyright © Microscopy Society of America 1998

References

References for peroxidase (DAB) staining:

Angermuller, S. and Fahimi, H.D.. 1981. Selective cytochemical localization of peroxidase, cytochrome oxidase and catalase In rat liver with 3,3'-diaminobenzidine. Histochemistry 71:3344.Google Scholar
Biggar, W.D. and Sturgess, J.M.. 1976, Peraxidase activity of alveolar macrophages. Lab. Invest. 34:31–42.Google ScholarPubMed
Breton-Gorius, J., Coquin, Y., and Guichard, J., 1978a, Cytochemical distinction between azuraphils and catalase-containing granules in leukocytes. I. Studies in developing neutrophils and monocytes from patients with myeloperoxidase deficiency: Comparison with peroxidase-deficient chicken heterophils, Lab. Invest. 38:21–31.Google ScholarPubMed
Breton-Gorius, J. and Guichard, J.. 1978b, Cytochemical distinction between azuraphils and catalase-containing granules in leukocytes: Distribution in human promyelocytes and promonocytes. J. Reticuloendothelial Soc. 21:637–646.Google Scholar
Cotran, R.S. and Litt, M.. 1970. Ultrastructural localization of horseradish peraxidase and endogenous peroxidase activity in guinea pig peritoneal macrophages. J. Immunol. 105:1536–1546.Google Scholar
Dunn, W.R., Hardin, J. H., Spicer, S. S.. 1968. Ultrastructural localization of myeloperoxidase in human neutrophil and rabbit heterophil and eosinophil leukocytes. Blood 32:935–944.Google Scholar
Fahimi, H.D. 1969. Cytochemical localization of peroxidatic activity of catalase in rat hepatic microbodies (peroxisomes), J. Cell. Biol. 43:275–288.CrossRefGoogle ScholarPubMed
Fahimi, H.D. 1979. An assessment of the DAB methods for cytochemical detection of catalase and peroxidase. J. Histochem. Cytochem. 27:1365–1366.Google Scholar
Graham, R.C. Jr. and Kamovsky, M.J.. 1966. The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: Ultrastructural cytochemistry by a new technique. J. Histochem. Cytochem. 14:291–302.Google Scholar
Kettle, A. J., Gedye, C.A., Hampton, M.B., Winterbourn, C.C.. 1995. inhibition of myeloperoxidase by benzoic acid hydrazides. Biochem. J. 308:559–563.CrossRefGoogle ScholarPubMed
Nishimura, E.T., Whest, G.M. and Yang, H.Y.. 1976. Ultrastructural localization of peroxidatic catalase in human peripheral blood leukocytes. Lab. Invest. 34:60–68.Google Scholar
Novikoff, A.B. and Goldfischer, S.. 1968. Visualization of microbodies for light and electron microscopy. Proc. Histochem. Soc. 16:507 (Abstract).Google Scholar
Novikoff, A.B. and Goldfischer, S.. 1969. Visualization of peraxisomes (microbodies) and mitochondria with diaminobenzidene, J. Histochem. Cytochem. 17(10) :675–680.CrossRefGoogle Scholar
Novikoff, A.B., Novikoff, P.M., Quintana, N., and Cleveland, D.. 1972. Diffusion artifacts in 3,3'-diaminobenzidene cytochemistry. J. Histochem. Cytochem. 20:745–749.Google Scholar
Roels, F., Wisse, E., De Prest, B.. and van der Meulen, J.. 1975. Cytochemical discrimination between cataiases and peroxidases using diaminobenzidene, Histochemistry 41:281–312.Google Scholar
Zellmer, D.M. and Shannon, W.A. Jr. 1983. Morphometric cytochemistry of catalase and myeloperoxidase-containing granules in the rabbit poiymorphonuclear leukocyte, Histochem. J. 15:211–230. CrossRefGoogle ScholarPubMed