title: Biochemical characterization of human myeloperoxidase using three specific monoclonal antibodies.
abstract: We have developed three monoclonal antibodies (moAbs), MA1, MA3 and MB1, which react with different antigenic determinants of human myeloperoxidase (MPO). In MPO-positive culture cell lines, HL-60 and NKM1, analysis of MPO by pulse-chase experiments followed by immunoprecipitation with these moAbs revealed that MPO was composed of subunits of 59K, 18K and 14.8K dalton polypeptides which are plausibly derived from the 89 K precursor. MA1 and MB1 react with both the precursor and the mature forms of MPO. MA3 reacts with only the mature forms of MPO. Blocking experiments on MPO-related functions revealed that the three moAbs could be divided into two groups. MA1 and MA3 inhibit MPO activities such as tetraguaiacol formation, iodide oxidation and luminol-dependent chemiluminescence, while MB1 shows no such inhibition.
mesh_terms: D000328:Adult; D000911:Antibodies, Monoclonal; D002460:Cell Line; D000939:Epitopes / Q000032:analysis; D006801:Humans; D007962:Leukocytes / Q000201:enzymology*; D009195:Peroxidase / Q000032:analysis* / Q000276:immunology / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D000939:Epitopes; D009195:Peroxidase