ArticleThe Korean journal of parasitology2000
Partial characterization of a 17 kDa protein of Clonorchis sinensis.
Article in The Korean journal of parasitology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Characterization of cysteine proteases from the carcinogenic liver fluke, Opisthorchis viverrini.Parasitology research · 2008Article
- Molecular cloning and immunolocalization of the 17 kDa myoglobin of Clonorchis sinensis.Parasitology research · 2003Article
- Excretory-secretory antigen is better than crude antigen for the serodiagnosis of clonorchiasis by ELISA.The Korean journal of parasitology · 2003Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
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Abstract
A 17 kDa protein from Clonorchis sinensis adults was purified by a procedure including Sephacryl S-200 HR gel filtration and Q-Sepharose anion exchange chromatography. The protein was proved to be a cysteine protease as it showed hydrolytic activity toward Cbz-Phe-Arg-AMC in the presence of dithiothreitol and was inhibited by specific inhibitors such as iodoacetic acid or trans epoxy-succinly-L-leucyl-amido(4-guanidino) butane. The polyclonal antibody raised against the protein reacted to 17 kDa proteins of trematodes such as Paragonimus westermani, Fasciola hepatica, Opisthorchis viverrini, Gymnophalloides seoi, and Metagonimus yokogawai. The antibody recognized the 17 kDa and 16 kDa cysteine proteases purified from C. sinensis, P. westermani, and G. seoi as well. These results suggest that the 17 kDa protein may be a cysteine protease commonly present in trematodes.
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