1. Glycosyl-phosphatidylinositol-specific phospholipase D Interaction with and stimulation by apolipoprotein A-I
- Author
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Reinhard Bolli, Urs Brodbeck, and Marius C. Hoener
- Subjects
Apolipoprotein B ,Biophysics ,Biochemistry ,Chromatography, Affinity ,chemistry.chemical_compound ,High-density lipoprotein ,Structural Biology ,Genetics ,Centrifugation, Density Gradient ,Phospholipase D ,Animals ,Phosphatidylinositol ,Molecular Biology ,chemistry.chemical_classification ,biology ,Apolipoprotein A-I ,Substrate (chemistry) ,Cell Biology ,Glycosyl-phosphatidylinositol ,Acetylcholinesterase ,Enzyme assay ,carbohydrates (lipids) ,Enzyme Activation ,Enzyme ,chemistry ,biology.protein ,Cattle ,lipids (amino acids, peptides, and proteins) ,Protein Binding - Abstract
Glycosyl-phosphatidylinositol-specific phospholipase D (GPI-PLD) is an amphiphilic protein which, in serum, is associated with high-density lipoproteins (HDL). It is shown that the major component of the HDL fraction, apolipoprotein A-I (apo A-I), is responsible for this association. In the absence of apo A-I, purified GPI-PLD occurred as virtually inactive aggregates which became disaggregated by apo A-I. The enzyme/apo A-I complex efficiently hydrolyzed the solubilized GPI-anchored substrate, acetylcholinesterase. Triton X-100 was also able to dissociate aggregated GPI-PLD, however, it strongly inhibited enzyme activity at detergent concentrations above the critical micellar concentration.
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