نتایج جستجو برای: liquid membrane solubilization
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Lipid rafts are localized mainly at the level of the plasma-membrane, but they can also form within internal membrane compartments, such as the Golgi appara-Lipid Rafts, Caveolae, and Caveolins For many years, scientists viewed the lipid bilayer of the tus (Gkantiragas et al., 2001). Therefore, the partitioning of caveolins into these liquid-ordered domains may be-plasma membrane as a two-dimen...
fonate (CHAPS) is a zwitterionic detergent that was specifically designed for membrane biochemistry. It is known to be a mild, nondenaturing detergent and is a derivative of natural bile salts. Its properties are of interest in several biochemical applications. These include the perturbation of membrane structures, membrane protein solubilization and functional reconstitution, and preparation o...
The human proteome project will demand faster, easier, and more reliable methods to isolate and purify protein targets. Membrane proteins are the most valuable group of proteins since they are the target for 70-80% of all drugs. Perbio Science has developed a protocol for the quick, easy, and reproducible isolation of integral membrane proteins from eukaryotic cells. This procedure utilizes a p...
Biological membranes are supposed to contain functional domains (lipid rafts) made up in particular of sphingomyelin and cholesterol, glycolipids, and certain proteins. It is often assumed that the application of the detergent Triton at 4 degrees C allows the isolation of these rafts as a detergent-resistant membrane fraction. The current study aims to clarify whether and how Triton changes the...
It has previously been shown that trypsinized triple-layered particles of rotavirus induce destabilization of liposomes and membrane vesicles in the absence of Ca2+, a condition which leads to solubilization of the outer capsid proteins of the virus. In this work, we have studied the relationship between outer capsid solubilization and permeabilization of membrane vesicles, monitoring particle ...
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