Abstract
Merozoites of malaria parasites have a membrane-bound serine protease whose solubilization and subsequent activity depend on a parasite-derived glycosylphosphatidylinositol-phospholipase C (GPI-PLC). The GPI-degrading activities from both Plasmodium falciparum and Plasmodium chabaudi have been characterized and partially purified by phenylboronate chromatography. They are membrane-bound, developmentally regulated, calcium-independent enzymes and as such they resemble GPI-PLC of Trypanosoma brucei. Furthermore, a T. brucei GPI-PLC-specific monoclonal antibody (mAT3) immunoprecipitates the plasmodial GPI-degrading activity. Thin-layer chromatography is suggestive of two activities: a GPI-PLC and a phospholipase A.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cross Reactions
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Glycolipids / metabolism*
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Glycosylphosphatidylinositol Diacylglycerol-Lyase
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Glycosylphosphatidylinositols
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Phosphatidylinositol Diacylglycerol-Lyase
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Phosphatidylinositols / metabolism*
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Phospholipases A / immunology
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Phospholipases A / isolation & purification
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Phospholipases A / metabolism*
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Phosphoric Diester Hydrolases / immunology
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Phosphoric Diester Hydrolases / isolation & purification
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Phosphoric Diester Hydrolases / metabolism*
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Plasmodium chabaudi / enzymology*
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Plasmodium falciparum / enzymology*
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Trypanosoma brucei brucei / enzymology
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Type C Phospholipases / immunology
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Type C Phospholipases / isolation & purification
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Type C Phospholipases / metabolism*
Substances
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Glycolipids
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Glycosylphosphatidylinositols
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Phosphatidylinositols
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Phospholipases A
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Phosphoric Diester Hydrolases
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Type C Phospholipases
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Phosphatidylinositol Diacylglycerol-Lyase
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Glycosylphosphatidylinositol Diacylglycerol-Lyase