Purification of a Plasmodium berghei neutral endopeptidase and its localization in merozoite.
A Plasmodium berghei neutral endopeptidase specific for the fluorogenic substrates valyl-leucyl-glycyl-arginyl/lysyl-aminoethyl-carbazole was purified by Fast Protein Liquid Chromatography. The enzyme was a Mr 68,000 polypeptide. Immunization of mice with the purified enzyme gave a specific antiserum, as demonstrated by immunoblotting. Immunofluorescence with this antiserum showed a strong labelling of P. berghei merozoites in mature segmented schizonts and of merozoites released from schizont-infected red blood cell. This labelling was mainly associated with the merozoite apex. It is possible that this endopeptidase is involved in the reinvasion.
Bernard
F
F
Laboratoire de Biologie Cellulaire, UA CNRS no. 290, Université de Poitiers, France.
Schrével
J
J
D000818:Animals; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D010962:Plasmodium berghei / Q000201:enzymology*; D013379:Substrate Specificity
D010450:Endopeptidases