Proteins

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino

Specificity:Trypsin cleaves peptides on the C-terminal side of lysine and arginine amino acid residues. If a proline residue is on the carboxyl side of the cleavage site, the cleavage will not occur. If an acidic residue is on either side of the