Chung, Y.B. 공윤 Cho, S.Y. Kang, S.Y. Choi, B.C. Lee, H.S. 2024-01-21T22:38:43Z 2024-01-21T22:38:43Z 2022-01-10 1993-01 0023-4001 https://pubs.kist.re.kr/handle/201004/146145 When activity of peroxidase in adult Paragonimus westermani was monitored using o-dianisidine and H2O2 as substrates, its specific activity was 1.5 times higher in excretory-secretory product (ESP) than in crude extract. The enzyme was purified by two purification steps of Sephacryl S-300 Superfine gel permeation and DEAE-Trisacryl M anion exchange chromatographies. Its activity increased 16.9 fold with 32.3% recovery. The enzyme was inhibited totally by 1 millimoles of dithiothreitol (DTT), 2-mercaptoethanol and azide. Molecular mass was 16 kDa in reducing SDS-polyacrylamide gel electrophoresis (PAGE) or 19 kDa in TSK-Blue gel filtration high performance liquid chromatography (HPLC), respectively. Special staining for peroxidase by diaminobenzidine on SDS-PAGE confirmed the activity. The peroxidase was less reactive to a paragonimiasis serum when observed by SDS-PAGE/immunoblot. In addition, specific activities of superoxide dismutase (SOD) and catalase were also identified in the ESP. High activities of these antioxidant enzymes in ESP indicate that they are parts of defense mechanisms against reactive oxygen intermediates from host. English Characterization of a peroxidase in excretory-secretory product of adult Paragonimus westermani. Article 10.3347/kjp.1993.31.3.259 1 The Korean journal of parasitology, v.31, no.3, pp.259 - 267 The Korean journal of parasitology 31 3 259 267 N scopus 2-s2.0-0027652659 Paragonimus westermani peroxidase SOD catalase excretory-secretory products