Abstract
The possibility of the use of saponin for permeabilization of synaptic vesicles from P2 fraction is explored. This fraction is isolated from rat brain cortex. Phosphorylation of membrane-bound proteins is performedin vitro. At the saponin:protein ratio 1:10 (w/w) phosphorylation of these proteins increases 2-fold due to increased membrane permeability for ATP and cAMP. Treatment of synaptic vesicles with saponin at the same ratio leads to the loss of cytosolic but not membrane-bound protein. This concentration of saponin can be used for permeabilization of other membranes, providing that the protein:cholesterol ratio is taken into consideration.
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