Korean J Parasitol.  1990 Sep;28(3):135-142. 10.3347/kjp.1990.28.3.135.

Purification of antigenic protein of sparganum by immunoaffinity chromatography using a monoclonal antibody

• Cho SY
• Kang SY
• Kong Y

• KMID: 1720301
• DOI: http://doi.org/10.3347/kjp.1990.28.3.135

Abstract

The quality improvement of antigen (crude saline extract) of Spirometra mansoni pleroceroid (sparganum) was investigated by protein purification. The crude extract was fractionated by gel filtration through Sephacryl S-300 Superfine. Its third fraction was purified by affinity chromatography using a monoclonal antibody as ligand. When observed by SDS-PAGE, the purified protein was composed of 2 bands of 36 kDa and 29 kDa which were found already as the most sensitive components in the crude extract by immunoblots with patients sera. The quality of the purified antigen was evaluated in comparison with the crude extract by enzyme-linked immunosorbent assay (ELISA) for the specific (IgG) antibody in sera of human sparganosis, other parasitic and neurologic diseases, and normal control. When the purified antigen was used, the sensitivity was not altered but remained high (96.4%) while the specificity was increased from 86.8% to 96.9%.

MeSH Terms

Antibodies,-Helminth-analysis
Antibodies,-Monoclonal
Antigens,-Helminth-diagnostic-use
Enzyme-Linked-Immunosorbent-Assay
IgG-analysis
Sparganosis-diagnosis
*Antigens,-Helminth-isolation-and-purification
*Chromatography,-Affinity
*Spirometra-immunology
Antibodies,-Helminth
Antibodies,-Monoclonal
Antigens,-Helminth