Myeloperoxidase, Human Polymorphonuclear Leukocytes

Native, human myeloperoxidase from polymorphonuclear leukocytes. A lysosomal enzyme that catalyzes oxidations by hydrogen peroxide, including MPO-chloride-mediated killing of microbes and tumor cells, inactivation of chemotactic factors, and cross-linking of proteins. MPO catalyzes the formation of hypochlorous acid that kills bacteria either by binding the halide ion to intracellular constituents or by oxidation of bacterial lipids and proteins.

Lyophilized from 100-700 mM NaCl, 50 mM sodium acetate buffer, pH 6.0.

Following reconstitution, aliquot and freeze (-20°C or -70°C). Stock solutions are stable for up to 1 year at -20°C or -70°C.

Further dilute in 100 mM NaCl, 50 mM sodium acetate, pH 6.0. Enzyme may precipitate out of solution in low ionic strength buffers or in distilled H₂O.

Nauseef, W.M., et al. 1998. J. Leukocyte Biol. 63, 264.
Panasenko, O.M., et al. 1994. Free Radic. Biol. Med. 16, 143.
Mulligan, M.S., et al. 1992. Br. J. Pharmacol.107, 1159.
Sharonov, B.P., and Churilova, I.V. 1992. Biochem. Biophys. Res. Commun.189, 1129.

One unit is defined as the amount of enzyme that will reduce 1.0 µmol H₂O₂ per min at 25°C, pH 6.0.

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Toxicity: Standard Handling (A)