We are trying to quantify protein encapsulated in liposomes. Since lipids in BCA interfere with the measurement, we need to perform a extraction and get rid off the lipids but with a good recovery of the protein. We tried some solvents to perform the extraction and so far methanol worked well. Our protein is highly hydrophilic. What are the best conditions to extract protein from liposomes using methanol? On the other hand we were thinking about breaking down the liposomes with a detergent (which one is the best one?) and the perform precipitation of the protein with TCA 50%/Acetone. In this case we need to select a good detergent that doesn't interfere with the following precipitation step with TCA 50%/Acetone. Finally, when we standardize the correct precipitation procedure we need to dissolve the protein again in water or PBS to perform the BCA analysis. We actually did a precipitation with methanol with good results but the protein made a pellet difficult to resuspend. We were thinking about heating, sonication, centrifugation adjustments but what are other options to enhance the solubilisation of the pellet protein again in PBS to quantify it? Thanks a lot for all your information.