Biochemical properties of a purified protein in cystic fluid of Taenia solium metacestodes.
- Author:
Seung Yull CHO
1
;
Suk Il KIM
;
Shin Yong KANG
;
Yoon KONG
Author Information
- Publication Type:Original Article
- MeSH: parasitology-helminth-cestoda; Taenia solium; metacestode; protein; antigen; cysticercus; biochemistry
- From:The Korean Journal of Parasitology 1988;26(2):87-94
- CountryRepublic of Korea
- Language:English
- 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)
