Korean J Parasitol.  2002 Jun;40(2):83-88. 10.3347/kjp.2002.40.2.83.

Characterization of partially purified 8 kDa antigenic protein of Clonorchis sinensis

  • 1Department of Parasitology and Institute of Endemic Diseases, Seoul National University College of Medicine, Seoul, Korea.
  • 2Department of Parasitology, College of Medicine, Cheju National University, Jeju, Korea.


The 8 kDa antigenic protein of Clonorchis sinensis was partially purified by ammonium sulfate precipitation and subsequently by a column chromatographic steps. The purified protein was separated into 7 and 8 kDa protein bands through SDS-tricine gel electrophoresis, while the protein was found to migrate to a 8 kDa band in 7.5-15% SDS-PAGE. The molecular weight of the antigen was estimated to be 110 kDa by Superose 6 HR 10/30 gel filtration. The purified antigen strongly reacted with the human sera of clonorchiasis. The hyperimmune sera of BALB/c mice immunized against the 8 kDa protein were reacted with both the crude extract and the excretory-secretory product of adult worms, but not with the metacercarial extract. Immunohistochemical staining demonstrated that the protein was distributed to the tegument and subtegumental cells and also to the seminal receptacle. The present findings suggest that the 8 kDa protein is a partition of the multicomplex protein originating from various organs of adult C. sinensis, and that it is composed of several 7 and 8 kDa proteins.


Clonorchis sinensis; 8 kDa antigen

MeSH Terms

Antigens, Helminth/immunology/*isolation & purification/metabolism
Clonorchis sinensis/anatomy & histology/*immunology/metabolism
Helminth Proteins/immunology/*isolation & purification/metabolism
Mice, Inbred BALB C
Molecular Weight
Support, Non-U.S. Gov't
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