Korean J Parasitol.
1988 Jun;26(2):87-94. 10.3347/kjp.1988.26.2.87.
Biochemical properties of a purified protein in cystic fluid of Taenia solium metacestodes
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- 1Department of Parasitology, College of Medicine, Chung-Ang University, Seoul 156-756, Korea.
- KMID: 1714941
- DOI: http://doi.org/10.3347/kjp.1988.26.2.87
Abstract
- By affinity chromatography using a monoclonal antibody as ligand, Kim et al. (1986) purified a protein fraction in cystic fluid of Taenia solium metacestodes (CF). In this study, the biochemical properties of the purified protein were characterized. Discontinuous-polyacrylamide gel electrophoresis (disc-PAGE) of the protein at 4.5~10% separating gel concentration showed its molecular weight (MW) to be 150 kilodalton(kDa) in non-denatured state, while denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed that it was composed of 3 different subunits with respective MW of 15, 10 and 7 kDa. Subunit of 7 kDa was shown to be linked to other subunits by disulfide bonds. Isoelectric point of the protein was pH 6.8. The protein was relatively heat-stable for immunologic analysis. These properties indicated that the protein, comprising about 70% of total content in CF, had similar biochemical characters with antigen B of Oriol et al.(1971) in hydatid cyst fluid (HF)
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