Trypsin Background

Trypsin was aboriginal declared in the backward 1800s as a proteolytic action present in pancreatic secretions. Subsequent studies appear that this agitator accurately anatomize peptide bonds C-terminal to the amino acerbic residues of lysine (Lys) and arginine (Arg) 109 times faster than hydrolysis by hydroxide ion. Since its antecedent discovery, trypsin has been articular in all animals, including insects, fish, and mammals. Trypsin from anniversary antecedent can alter hardly in activity, but the accustomed substrate for the agitator is about any peptide that contains Lys or Arg. The specificity of trypsin allows it to serve both digestive and authoritative functions. As a digestive agent, it degrades ample polypeptides into abate fragments. As a authoritative protease, it activates added proteins through proteolysis at specific Lys or Arg bonds.
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Rat trypsin ELISA Kit