Cysteine proteinase activity in various developmental stages of Clonorchis sinensis: a comparative analysis.
1. Cysteine proteinase activity in acidic extracts of various developmental stages of Clonorchis sinensis (metacercariae, 1-, 2-, and 3-month old worms) was examined. All the activities were maximum at acidic pH and showed inhibitor susceptibilities similar to the vertebrate cysteine proteinases. 2. Specific activity of cysteine proteinase(s) was highest in metacercariae with either CBZ-phe-arg-AFC or Azocoll as the substrate. The immature and mature worms had similar (but less than metacercariae) levels of activity. 3. A soluble cysteine proteinase with a native molecular weight of approximately 20,000 +/- 1414 was partially purified from 1-, 2-, and 3-month worms. The molecular weight of similar activity in metacercariae was approximately 32,000. 4. Results suggest developmental regulation of cysteine proteinase activity in the life cycle of C. sinensis.
Song
C Y
CY
Department of Biology, Chung-Ang University, Seoul, Korea.
Rege
A A
AA
D000818:Animals; D002850:Chromatography, Gel; D003004:Clonorchis sinensis / Q000201:enzymology* / Q000254:growth & development; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology
D015853:Cysteine Proteinase Inhibitors; D003546:Cysteine Endopeptidases