Component proteins in crude extract of adult Paragonimus westermani purified by immunoaffinity chromatography using monoclonal antibodies.
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.
Kang
S Y
SY
Department of Parasitology, College of Medicine, Chung-Ang University, Seoul, Korea.
Kong
Y
Y
Cho
S Y
SY
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D002846:Chromatography, Affinity; D004848:Epithelium / Q000737:chemistry; D015801:Helminth Proteins / Q000302:isolation & purification*; D007422:Intestines / Q000737:chemistry; D051379:Mice; D008807:Mice, Inbred BALB C; D010238:Paragonimus / Q000737:chemistry*; D014020:Tissue Extracts / Q000032:analysis
D000911:Antibodies, Monoclonal; D015801:Helminth Proteins; D014020:Tissue Extracts