Detecting Carbamylation of Intact Proteins and Peptides by LC/MS (/MS)

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Part Number:
Paul Rainville, Kefei Zheng, Claude Mallet, Reb Russell II [Waters]
FAll ACS 2002; 224th ACS National Meeting; Boston August 18-22
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Content Subtype:
Protein; Peptide; Bovine Cytochrome C; Carbonic Anhydrase; Horse Heart Myoglobin
Symmetry300(™) C18 300 Å 5 µm Steel 4.6 mm 50 mm Atlantis dC18 3 µm Steel 4.6 mm 50 mm
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Characterization of pharmaceutical proteins is an important analytical challenge that must be met in pharmaceutical and biotechnology companies today. Small chemical variations in proteins can be the difference between an active and an inactive therapeutic. Reversed-phase chromatography coupled with mass spectrometry has rapidly become the technique of choice for the determination of post translation modifications. We have developed a simple and rapid LC/MS method for identifying the presence and degree of carbamylation of intact proteins or peptides in a mixed sample using either single quadrupole or Q-TOF type instrumentation.

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