Purification and identification of a neutral endopeptidase in Plasmodium falciparum schizonts and merozoites.

Abstract:

:An endopeptidase specific to the Plasmodium falciparum erythrocytic schizont stage and to free merozoites was detected using the fluorogenic GlcA-Val-Leu-Gly-Lys(or Arg)-AEC substrate. The enzyme was purified by high performance liquid chromatography (HPLC); its optimal activity was around pH 7.5 and its isoelectric point was 4.4. The molecular weight of the enzyme was about 68,000, as demonstrated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. The endopeptidase was strongly inhibited by thiol proteinase inhibitors, leupeptin, and antipain. The possible involvement of this neutral endopeptidase in the reinvasion process is discussed.

journal_name

Parasitol Res

journal_title

Parasitology research

authors

Grellier P,Picard I,Bernard F,Mayer R,Heidrich HG,Monsigny M,Schrével J

doi

10.1007/BF00930972

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

455-60

issue

6

eissn

0932-0113

issn

1432-1955

journal_volume

75

pub_type

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