title: Biochemical properties of a purified protein in cystic fluid of Taenia solium metacestodes.
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)
authors.affiliation: Department of Parasitology, College of Medicine, Chung-Ang University, Seoul, 156-756, Korea.
authors.forename: Seung Yull
authors.initials: SY
authors.lastname: Cho
authors.forename: Suk Il
authors.initials: SI
authors.lastname: Kim
authors.forename: Shin Yong
authors.initials: SY
authors.lastname: Kang
authors.forename: Yoon
authors.initials: Y
authors.lastname: Kong