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. 1972 Feb;66(2):277–294.

Ultrastructural Localization of Peroxidase Activity in Human Platelets and Megakaryocytes

Janine Breton-Gorius, Josette Guichard
PMCID: PMC2032483  PMID: 5009974

Abstract

Normal human platelets and megakaryocytes were examined for peroxidase activity by the diaminobenzidine (DAB) cytochemical technic. When the fixation and the incubation were adequate, a strong reaction was present in the dense tubular system of platelets suspended in plasma or spread on carbon. The black reaction product was ascribed to enzyme activity, since the reaction was completely eliminated when H2O2 or DAB were omitted, or when H2O2 was in excess. In addition, the reaction was inhibited by aminotriazole, cyanide and azide. In the human megakaryocytes, the reaction was localized in the endoplasmic reticulum including the perinuclear envelope. The Golgi complex and the clear vacuolar system were negative for the reaction. After platelet release, the reaction was always seen in the perinuclear space. The nature and function of the enzyme, as well as its possible relationships with catalase, are discussed.

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Selected References

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