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Antigens of Plasmodium lophurae *
Author(s) -
SHERMAN IRWIN W.
Publication year - 1964
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1964.tb01772.x
Subject(s) - hemozoin , precipitin , antigenicity , lysis , antigen , plasmodium (life cycle) , biology , starch , parasite hosting , urea , biochemistry , antiserum , chemistry , microbiology and biotechnology , enzyme , immunology , heme , world wide web , computer science
SYNOPSIS. Erythrocyte‐free Plasmodium lophurae were lysed by freeze‐thawing and the lysate subjected to contrifugation. Two fractions were obtained: (1) hemozoin, an insoluble protein‐containing pigment and (2) soluble proteins. Hemozoin when “solubilized” in 4 M urea was immobile upon electro‐phoresis in a 4 M urea starch gel. The soluble plasmodial proteins were grossly contaminated by host cell hemoglobin, but were readily separated from the latter by starch gel electrophoresis. Employment of the Ouchterlony and immunoelectrophoretic techniques demonstrated that one of the major antigenic components in this avian plasmodium is hemoglobin. The malarial pigment showed no antigenicity. Rabbit antisera prepared against formalinized erythrocyte‐free parasites discerned some 4 to 6 precipitating antigens, but no such reaction was obtained using hyperimmune chicken serum after naturally induced blood infections. These studies show the distinct nature of the host and parasite by physico‐chemical means and illustrate the value of the immunoelectrophoretic method in providing a simple and sensitive tool for detecting impurities in parasite protein preparations. It is further suggested that confusion in host and parasite antigens as described in the literature may in part be due to these unidentified erythrocyte elements.