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Clonorchis sinensis: purification and characterization of a cysteine proteinase from adult worms.

作者信息

Song C Y, Dresden M H, Rege A A

机构信息

Department of Biology, Chung-Ang University, Seoul, Korea.

出版信息

Comp Biochem Physiol B. 1990;97(4):825-9. doi: 10.1016/0305-0491(90)90129-h.

Abstract
  1. Adult Clonorchis sinensis, the Chinese liver fluke, is known to migrate to the bile ducts of its mammalian host and cause significant pathology. 2. An acidic, thiol-dependent proteinase with a native mol. wt of approximately 18,500 was purified to homogeneity using ion-exchange chromatography and gel filtration chromatography. By SDS-polyacrylamide gel electrophoresis, the mol. wt of the enzyme was estimated to be 15,000. 3. The enzyme was similar to cathepsin B-like cysteine proteinases based on pH optimum, substrate specificity, and inhibitor sensitivity. 4. Antisera from human clonorchiasis and C. sinensis-infected rabbits reacted in immunoblots with the partially purified proteinase. The C. sinensis proteinase may be useful for serodiagnosis of clonorchiasis.
摘要

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