Chapter title |
Binding of Serpins to Immobilized Phospholipids and Phospholipids in Suspension
|
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Chapter number | 8 |
Book title |
Serpins
|
Published in |
Methods in molecular biology, September 2018
|
DOI | 10.1007/978-1-4939-8645-3_8 |
Pubmed ID | |
Book ISBNs |
978-1-4939-8644-6, 978-1-4939-8645-3
|
Authors |
Felix C. Wahlmüller, Judit Mihaly-Bison, Margarethe Geiger, Wahlmüller, Felix C., Mihaly-Bison, Judit, Geiger, Margarethe |
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. |
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