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- W2890742954 abstract "Binding of serine protease inhibitors (serpins) to nonprotein ligands such as glycosaminoglycans or phospholipids has been shown to modify their inhibitory activity and-at least in the case of SERPINA5-to mediate serpin internalization into cells. Also phospholipid functions may be altered when bound to serpins or other proteins.By interacting with phospholipids, serpins might influence a variety of cellular functions. Binding of proteins to phospholipids can be studied by several methods. Here we describe solid-phase assays, in which pure phospholipids are immobilized on nitrocellulose membranes, PVDF membranes, or microtiter plates. Bound proteins are detected with specific antibodies and labeled secondary antibodies. We also describe a method visualizing binding of phospholipids in suspension by non-denaturing polyacrylamide gel electrophoresis (PAGE) followed by Western blotting." @default.
- W2890742954 created "2018-09-27" @default.
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- W2890742954 date "2018-01-01" @default.
- W2890742954 modified "2023-10-18" @default.
- W2890742954 title "Binding of Serpins to Immobilized Phospholipids and Phospholipids in Suspension" @default.
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- W2890742954 doi "https://doi.org/10.1007/978-1-4939-8645-3_8" @default.
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- W2890742954 hasPublicationYear "2018" @default.
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