• Parasites, Hosts and Diseases
• /
• v.28 no.2
• /
• pp.101-108
• /
• 1990

Surgically collected cystic fluid of Taenia solium metacestodes from patients of intracranial cystic lesion were compared in their protein composition with those from naturally infected pigs in Cheju Do, Korea and Ecuador. In non-denaturing discontinuous-polyacryla aide gel electrophoresis (disc-PAGE) , no discernible differences were recognized in banding patterns between the cystic fluids from Cheju Do and Ecuador, and between the cystic quids from pigs and human lesions except wider bands that corresponded to human albumin and T-globulin (in 4 of 9 patients). In reducing SDS-PAGE, bands in the cystic Ruid from Ecuador showed the same banding pattern with that from Cheju Do but two bands of 21 and 17 kDa were stained darker. Cystic quids (rom patients revealed the same protein compositions of the major protein bands of 94, 64, 15, 10 and 7 kDa as in the cystic fluid of pig origin, but human albumin (66 kDa), heavy and light chains of gamma globulin (55 and 22.5 kDa) were contaminated in 4 of 9 cystic fluids. Human CSF proteins seem to have been contaminated during cystic ftuid collection. In any cystic quid from patients, the majcr Protein component was 150 kDa which was subdivided into 15, 10 and 7 kDa in reducing SDS-PAGE.

• Parasites, Hosts and Diseases
• /
• v.29 no.2
• /
• pp.113-120
• /
• 1991

When the component proteins in crude saline extract of 13-week old adult Paragonimus westermani were observed by non-denaturing discontinuous-polyacrylamide gel electrophoresis (Disc-PAGE), 8 distinct bands were clearly recognized. Molecular weight (MW) of each band protein, numbered in sequence from cathodal side which appeared in 10% separating gel, was measured first by Ferguson plot utilizing different gel concentrations from 10% to 4.5%. MW of band 1 Protein (known as egg Protein) was 440 kDa. And MW of other band Proteins were: 386 kDa in band 2, 17.4 kDa in band 3, 17kDa in band 4, 14.3 kDa in band 5, 46 kDa in band 6, 38 kDa in band 7 and 23 kDa in band 8. When the proteins in the crude extract were separated into fractions by molecular sieve chromatography through 1.6 (Φ)×70cm sired Sephacryl 5-300 Superane column and revisualized by Disc-PAGE in 8% gel, the sequence of fluted proteins was band 1, band 2, band 6, band 7 and bands 3,4,5 and 8. This elusion profile confirmed MW of each band protein in the crude extract as measured by Ferguson plot.

• Parasites, Hosts and Diseases
• /
• v.26 no.2
• /
• pp.87-94
• /
• 1988

By affinity chromatography using a monoclonal antibody as ligand, Kim et at. (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 suifate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed that it was composed of 3 different subunits with respective fnw of 15, 10 and 7 kDa. Subunit of 7 kDa was shown to be linked to other subunits by disulade 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 at.(1971) in hydatid cyst quid (HF).