Fast On-Line Desalting of Proteins for Determination of Structural Variation Using Exact Mass Spectroscopy

by Thomas E. Wheat, PhD, Paul R. Rainville, Beth L. Gillece-Castro, Ziling Lu, Laetitia Cravello, and Jeffrey R. Mazzeo
Volume 6, Issue 1 (Spring 2007)

Analytical tools for the characterization of protein identity and structure are fundamental to many fields of biochemical research. For the development of protein biopharmaceuticals, it is particularly important to measure modifications of the structure that may affect safety and efficacy. This application requires the analysis of large numbers of samples during process development. Small quantities of modifications must be detected in samples that are in the presence of more abundant native protein. Many kinds of analytical techniques are applied to this problem including peptide mapping, bioassays, liquid chromatography, spectroscopy, and so on. One of the most attractive tools is mass spectrometry, since essentially any change in the molecule is accompanied by a change in molecular weight. With the recent advent of readily accessible mass spectrometers capable of routine exact mass measurement, it is appropriate to consider the detailed requirements for this application…

Citation:
Wheat TE, Rainville PR, Gillece-Castro BL, Lu Z, Cravello L, Mazzeo JR. Fast On-Line Desalting of Proteins for Determination of Structural Variation Using Exact Mass Spectroscopy. BioProcess J, 2007; 6(1): 55-59. http://dx.doi.org/10.12665/J61.Wheat