Detergents have been used to enhance the soly. of hydrophobic biomols. for decades. Despite the widespread use of detergents in biochem., the presence of these mols. often complicates further anal. by mass spectrometry. This study presents a soln. to this problem by outlining a method utilizing a novel cleavable detergent, 3-[3-(1,1-bisalkyloxyethyl)pyridin-1-yl]propane-1-sulfonate (PPS). This detergent can be used to ext. protein contained within the interior of the cell by disrupting cell membranes. Once the proteins are free from the cell, PPS also assists in protein solubilization by shielding the hydrophobic regions of the newly extd. protein from unfavorable interactions with water. The added advantage of PPS over conventional detergents such as SDS or n-octylglucoside is that the detergent properties that interfere with MALDI mass spectrometry can be eliminated prior to anal. PPS was found to improve sensitivity in MALDI analyses of both sol. proteins and membrane proteins without degrading spectral quality. The virtues of this strategy were applied to whole cell exts. Anal. of these exts. resulted in an overall increase in both the no. of peaks obsd. and overall signal intensity.
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