Pagels W R, Sachs R J, Marnett L J, Dewitt D L, Day J S, Smith W L
J Biol Chem. 1983 May 25;258(10):6517-23.
Monoclonal antibodies against prostaglandin H (PGH) synthase have been used to precipitate cyclooxygenase and peroxidase activities from detergent-solubilized preparations of ram seminal vesicle microsomes. Approximately 85% of the solubilized cyclooxygenase activity was precipitated using an excess of anti-PGH synthase antibody; under similar conditions, immunoprecipitation of 60% of the diphenylisobenzofuran peroxidase, 75% of the phenylbutazone peroxidase, and 50% of the epinephrine peroxidase activities occurred. In contrast, less than 10% of the cyclooxygenase or peroxidase activities could be precipitated with nonimmune, control antibody preparations. These data indicate that the hydroperoxidase activity of PGH synthase is the major peroxidase activity catalyzing the co-oxidation of xenobiotics in ram seminal vesicle microsomes.
抗前列腺素H（PGH）合酶的单克隆抗体已被用于从去污剂增溶的公羊精囊微粒体制剂中沉淀环氧化酶和过氧化物酶活性。使用过量的抗PGH合酶抗体可沉淀约85%的增溶环氧化酶活性；在类似条件下，可免疫沉淀60%的二苯基异苯并呋喃过氧化物酶、75%的保泰松过氧化物酶和50%的肾上腺素过氧化物酶活性。相比之下，用非免疫对照抗体制剂沉淀的环氧化酶或过氧化物酶活性不到10%。这些数据表明，PGH合酶的氢过氧化物酶活性是催化公羊精囊微粒体中外源化合物共氧化的主要过氧化物酶活性。
