Improved Tryptic Digestion of Proteins Via a Novel Solubilization Factor

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Part Number:
Ying Qing Yu, Martin Gilar, Peter J. Lee, Weibin Chen, John C. Gebler [Waters]
ASMS 2002; Orlando; 4 June 2002
Content Type:
Content Subtype:
Proteins, Protein Digest, Trypsin, BAEE, Tryptic Digest, Myoglobin, Bovine Ubiquitin, Amino Acids, Ovalbumin, Bacteriorhodopsin, Bovine Serum Albumin, BSA, BA
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Rapid advancements in mass spectrometry field enable more sensitive and accurate identification of proteins. However, hydrophobic proteins are troublesome to identify by mass spectrometric method due to their low solubility. Surfactants are commonly used to disrupt the aggregation of hydrophobic biomolecules prior to enzymatic digestions; however, ionic surfactants such as SDS are disruptive to enzyme activity and interfere with the mass spectrometry detection. We employed a novel acid-labile surfactant (ALS) for enzymatic digestion of proteins. Drastic improvement of protein digestion in terms of speed and peptide recovery is observed. Mild acidic condition breaks down ALS to MS non-interfering byproducts, providing additional advantages of this surfactant for MS characterization of proteins/peptides.

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