Purification and immunologic reactivity of Hymenolepis diminuta surface antigens.
The outer part of Hymenolepis diminuta tegument was extracted with 3 M KCl. The antigen was adsorbed from the extract on an affinity column containing H. diminuta-infected rat immunoglobulin immobilized on Sepharose 4B and could be eluted with 2.5 M urea at pH 2.8. Analysis of polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of both the crude extract and material eluted from the column showed that the latter was markedly purified. Double diffusion and immunoelectrophoresis revealed 11 and 4 antigenic components in the crude extract and purified preparation, respectively.
Krawczuk
S
S
Institute of Parasitology, Polish Academy of Sciences, Warszawa, Poland.
Rode
W
W
Machnicka
B
B
D000818:Animals; D000947:Antigens, Helminth / Q000276:immunology / Q000302:isolation & purification*; D000954:Antigens, Surface / Q000276:immunology / Q000302:isolation & purification; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006926:Hymenolepis / Q000276:immunology*; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007136:Immunoglobulins / Q000276:immunology; D008297:Male; D051381:Rats
D000947:Antigens, Helminth; D000954:Antigens, Surface; D007136:Immunoglobulins