ACTIVITY OF INTRACELLULAR PHOSPHOLIPASE A1AND A2IN GIARDIA LAMBLIA
Giardia lamblia
Giardia
DOI:
10.1645/ge-1038r3.1
Publication Date:
2007-11-15T19:00:49Z
AUTHORS (8)
ABSTRACT
Neither phospholipase A1 (PLA A1) nor A2 A2), their respective genes, have been identified in Giardia lamblia, even though they are essential for lipid metabolism this parasite. A method to identify, isolate, and characterize these enzymes is needed. The activities of PLA were analyzed a total extract (TE) vesicular (P30) soluble (S30) subcellular fractions G. lamblia trophozoites; the effects several chemical physicochemical factors on investigated. assays performed using substrate labeled with 14C, mass 14C-product was quantified. activity present TE P30 S30 fractions, it dependent pH concentrations protein Ca2 . In all trophozoite preparations, inhibited by ethylenediaminetetraacetic acid Rosenthal's inhibitor. These results suggest that possesses isoforms may be or associated membranes. addition participating phospholipid metabolism, could play important roles cytopathogenicity
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