Purification and identification of a neutral endopeptidase inPlasmodium falciparum schizonts and merozoites
- 1 January 1989
- journal article
- research article
- Published by Springer Nature in Zeitschrift Fur Parasitenkunde-Parasitology Research
- Vol. 75 (6) , 455-460
- https://doi.org/10.1007/bf00930972
Abstract
An endopeptidase specific to thePlasmodium 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 68000, 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.Keywords
This publication has 41 references indexed in Scilit:
- Plasmodium falciparum Malaria: Band 3 as a Possible Receptor During Invasion of Human ErythrocytesScience, 1985
- Detection and characterization of a selective endopeptidase from Plasmodium berghei by using fluorogenic peptidyl substratesBiochemical and Biophysical Research Communications, 1984
- Sensitive fluorometric determination of plasminogen activator in cell lysates and supernatantsFEBS Letters, 1983
- Erythrocytes deficient in glycophorin resist invasion by the malarial parasite Plasmodium falciparumNature, 1982
- Identification of Surface Proteins on Viable Plasmodium knowlesi MerozoitesThe Journal of Protozoology, 1981
- Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasiteThe Journal of cell biology, 1978
- Human Malaria Parasites in Continuous CultureScience, 1976
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970