Korean J Parasitol.  2000 Jun;38(2):95-97. 10.3347/kjp.2000.38.2.95.

Partial characterization of a 17 kDa protein of Clonorchis sinensis

• Chung YB
• Chung BS
• Choi MH
• Chai JY
• Hong ST

• KMID: 1715242
• DOI: http://doi.org/10.3347/kjp.2000.38.2.95

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.

MeSH Terms

Animal
Clonorchis sinensis/enzymology*
Cysteine Endopeptidases/metabolism*
Cysteine Endopeptidases/isolation & purification
Cysteine Endopeptidases/chemistry
Helminth Proteins/metabolism*
Helminth Proteins/isolation & purification
Helminth Proteins/chemistry
Molecular Weight