(2014) Comprehensive tracking of host cell proteins during monoclonal antibody purifications using mass spectrometry, mAbs, 6:3, 659-670,

The high mobility group (HMG) proteins, including HMGA, HMGB and HMGN, are abundant and ubiquitous nuclear proteins that bind to DNA, nucleosome and other multi-protein complexes in a dynamic and reversible fashion to regulate DNA processing in the context of chromatin. All HMG proteins, like histone proteins, are subjected to extensive post-translational modifications (PTMs), such as lysine acetylation, arginine/lysine methylation and serine/threonine phosphorylation, to modulate their interactions with DNA and other proteins. There is a growing appreciation for the complex relationship between the PTMs of HMG proteins and their diverse biological activities. Here, we reviewed the identified covalent modifications of HMG proteins, and highlighted how these PTMs affect the functions of HMG proteins in a variety of cellular processes.

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Porous silicon powder and silica gel particles have been applied as inorganic matrices for the analysis of small molecules in matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐TOFMS). In contrast to conventional MALDI‐TOFMS, the signal interference of low‐molecular analytes by the matrix has been eliminated. Almost no fragmentations of the analytes were observed. Effects of various factors, such as the particle and pore size, the suspending solution, and sample preparation procedures, on the intensity of mass spectra have been investigated. The pore structure of the inorganic matrix and penetration of the analytes into the pores must be optimized for effective desorption and ionization of the analytes. Matrices (DHB and HCCA) were covalently bound to silica gel for improvement of spectrum intensity. Copyright © 2001 John Wiley & Sons, Ltd.