Immunoprecipitation of malarial acid endopeptidase.
Electrophoresis of extracts of schizonts of Plasmodium knowlesi in non-dissociating polyacrylamide gels, separates several bands of acid endopeptidase activity. A polyclonal antiserum, produced by immunization with purified merozoites, failed to distinguish between different bands of the parasite enzyme, indicating that they are serologically related. Apart from the loss of one minor peak, extraction in Triton X-100 did not reduce the enzyme's electrophoretic heterogeneity. The antiserum did not react with red cell acid proteases.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D007106:Immune Sera / Q000276:immunology; D007114:Immunization; D007123:Immunoelectrophoresis, Two-Dimensional; D007124:Immunoenzyme Techniques; D008254:Macaca nemestrina; D017830:Octoxynol; D010961:Plasmodium / Q000201:enzymology* / Q000276:immunology; D011092:Polyethylene Glycols
D007106:Immune Sera; D011092:Polyethylene Glycols; D017830:Octoxynol; D010450:Endopeptidases