Final answer:
The assertion that GPI-anchored proteins can be extracted from the membrane using high salt is false, as these proteins typically require the use of detergents or phospholipases due to their strong membrane anchoring.
Step-by-step explanation:
Extraction of GPI-anchored Proteins
The statement that GPI-anchored proteins can be extracted from the membrane using high salt is False. GPI-anchored proteins, which are attached to the membrane via a glycosylphosphatidylinositol (GPI) anchor, typically require other methods for extraction, such as the use of detergents or phospholipases. High salt conditions can affect proteins differently based on their solubility characteristics and the nature of their interactions with other cellular components. While high salt can be used to elute certain proteins from cell walls or to dissociate proteins non-covalently associated with chromatin, GPI-anchored proteins are not easily extracted purely by salting-out techniques because of the strong anchoring to the membrane. To release GPI-anchored proteins, one usually needs to break down the GPI anchor specifically, not just disrupt protein-protein interactions.
In contrast to GPI-anchored proteins, there are examples of peripheral proteins like cytochrome c that can readily dissociate from membranes under high salt conditions. Salt solutions, such as CaCl2, have been used successfully to extract certain cell wall proteins (CWPs), but GPI-anchored proteins are not typically released by this method. Structural proteins covalently linked to membranes require more forceful methods to solubilize, and thus are not well represented in cell wall proteomic studies based on salt extraction techniques.