Trypsin-ultra, Mass Spectrometry Grade is a serine endopeptidase, which selectively cleaves peptide bonds C-terminal to lysine and arginine residues. Trypsin-ultra cleaves at Lys-Pro and Arg-Pro bonds at a much slower rate than when Lys and Arg are N-terminal to other residues.
Trypsin-ultra™, Mass Spectrometry Grade is a serine endopeptidase. It selectively cleaves peptide bonds C-terminal to lysine and arginine residues (1). Trypsin-ultra is treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone (TPCK) to inactivate any remaining chymotryptic activity. It is modified by acetylation of the ε-amino groups of lysine residues to prevent autolysis. Trypsin-ultra (TPCKtreated) cleaves at Lys-Pro and Arg-Pro bonds at a much slower rate than other amino acid residues (2).
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