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- W1556639392 abstract "This chapter investigates the interaction of the GM2 activator protein with sulfated and sialylated glycosphingolipids. Data concerning the interaction of GM2AP with gangliosides were obtained from biophysical measurements. The membrane activity of GM2AP was measured by high-sensitivity differential scanning calorimetry (DSC) and film balance measurements, as well as by surface plasmoresonance studies. Analytical techniques such as thin-layer chromatography (TLC) overlay and fluorescence dequenching techniques provided evidence for the specific interaction between the lipid-binding protein and gangliosides. By TLC overlay it was shown that GM2AP bound to GM1, the precursor of GM2 in ganglioside catabolism; GM2 itself; and GM3, the product of GM2 degradation. In vivo, the GM2AP is required for the degradation of ganglioside GM2 and glycolipid GA2, as well as for the sufficient degradation of glycolipid SM2a. In vitro it also acts on related GSL, such as GM1 or globotetraosylceramide. Binding and transfer studies suggested that this cofactor acts as a liftase, –it recognizes its lipid substrate, complexes it, and lifts it out of the membrane plane, thus presenting it to the water-soluble enzyme for degradation." @default.
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- W1556639392 date "2003-01-01" @default.
- W1556639392 modified "2023-09-25" @default.
- W1556639392 title "Interaction of the GM2 Activator Protein with Sulfated and Sialylated Glycosphingolipids" @default.
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- W1556639392 doi "https://doi.org/10.1016/s0076-6879(03)01053-x" @default.
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