Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues. Typically there is little or no cleavage at arginyl-proline and lysyl-proline bonds. This trypsin is purified from bovine pancreas, 1X crystallized, dialyzed against 1mM HCl and lyophilized. >150 TAME untis/ mg protein. One Unit hydrolyzes 1µmole of p-toluene-sulfonyl-L-arginine methyl ester (TAME) per minute at 25°C, pH 8.2, in the presence of 10mM calcium.
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