Korean J Parasitol.  1991 Dec;29(4):363-369. 10.3347/kjp.1991.29.4.363.

Component proteins in crude extract of adult Paragonimus westermani purified by immunoaffinity chromatography using monoclonal antibodies

• Kang SY
• Kong Y
• Cho SY

• KMID: 1715540
• DOI: http://doi.org/10.3347/kjp.1991.29.4.363

Abstract

The nature of 2 component proteins in crude saline extract of adult Paragonimus westermani was investigated. By immunoaffinity chromatography using monoclonal antibodies (MAb) as ligands, the proteins were purified from the crude extract. Band 1 protein in disc-polyacrylamide gel electrophoresis (PAGE) was purified by PFCK-136 MAb. The protein, known to have molecular mass of 440 kDa, was composed of 23, 46 and 92 kDa subunits when observed by reducing SDS-PAGE and SDS-PAGE/immunoblot. This protein was originated from eggs of the worm as revealed by immunohistochemical staining with PFCK-136 Mab. Another affinity purified protein utilizing PFCK-44 MAb was the band 4 protein of 17 kDa in disc-PAGE. This was a monomer protein in reducing SDS-PAGE and SDS-PAGE/immunoblot. The protein was produced at intestinal epithelium of the worm.

MeSH Terms

Chromatography,-Affinity
Epithelium-chemistry
Intestines-chemistry
Mice-
Mice,-Inbred-BALB-C
Tissue-Extracts-analysis
*Antibodies,-Monoclonal-immunology
*Helminth-Proteins-isolation-and-purification
*Paragonimus-chemistry
Antibodies,-Monoclonal
Helminth-Proteins
Tissue-Extracts