A Method For Detecting Post Translational Modifications In Intact Proteins and Peptides.

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Reb J. Russell II;Paul Rainville;Claude Mallet;Kefei Zheng;Jeff Mazzeo[Waters]
Fall ACS 2002; 224th ACS National Meeting; Boston August 18-22
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Protein; Peptide; Lysine; Arginine; Cysteine; Myoglobin; Cytochrome C; beta Casein; alpha Casein
Symmetry300(™) C18 300 Å 5 µm Steel 4.6 mm 50 mm Symmetry® C18 5 µm Steel 4.6 mm 50 mm Delta-Pak C18 300 Å 5 µm Steel 4.6 mm 50 mm Atlantis dC18 3.5 µm Steel 4.6 mm 50 mm
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Characterization of pharmaceutical proteins and peptides is an important analytical challenge that must be met in pharmaceutical and biotechnology companies today. Small chemical variations in proteins and peptides can be the difference between an active and an inactive therapeutic. In this study, we looked as some of the more common modifications; carbamylation, oxidation, formylation, deamidation, and acylation that are a byproduct of production, purification, and/or formulation. We have developed a comprehensive and rapid LC/MS methodology that can indicate the presence and degree of posttranslational modification using intact proteins or peptides. Our methodology is based on reversed-phase chromatography coupled with mass spectrometry since LC-MS is becoming a choice for the determination of post translation modifications.

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