Factors influencing myeloperoxidase and catalase activities in polymorphonuclear leukocytes.

摘要: Abstract 1. Various factors affecting myeloperoxidase (EC 1.11.1.7) and catalase 1.11.1.6) activities in polymorphonuclear leukocytes have been investigated. 2. Under conditions which the myeloperoxidase-containing granules of remain intact, such as intact cells or 0.25 M sucrose homogenates, is not inhibited by 3-amino-1,2,4-triazole endogenously generated H2O2. Catalase aminotriazole but H2O2 under conditions. When are disrupted, phagocytizing cells, homogenates that frozen thawed sucrose-free both enzymes aminotriazole. Exogenous H2O2, at concentrations employed us, inhibits frozen-thawed homogenates. Aminotriazole also purified myeloperoxidase. 3. Myeloperoxidase activity was 18 times greater lysed versus granule preparations. 4. It postulated myeloperoxidase, like lysosomal enzymes, probably inactive resting might function following lysis containing granules. A possible role regulation suggested.