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

Autor: Song CY; Department of Biology, Chung-Ang University, Seoul, Korea., Dresden MH, Rege AA
Jazyk: angličtina
Zdroj: Comparative biochemistry and physiology. B, Comparative biochemistry [Comp Biochem Physiol B] 1990; Vol. 97 (4), pp. 825-9.
DOI: 10.1016/0305-0491(90)90129-h
Abstrakt: 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.
Databáze: MEDLINE