Trypsin

Trypsins are a type of enzyme that often function as digestive enzymes in humans and other vertebrates. They are a type of protease which means they act by helping to break bonds between amino acids in proteins. Digestive trypsins are part of an intermediate stage of protein digestion, where they cut long chains of amino acids into smaller pieces near the start of the small intestines. More generally, trypsins are serine protease enzymes from the PA clan superfamily, and in humans there are three classical varieties: trypsin 1, 2, and 3. Trypsins are formed in the small intestines when their pancreas-produced proenzymes, known as trypsinogens, are activated with the help of enteropeptidase, a protease found in the intestines. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine and arginine. It is widely used in numerous biotechnology applications in clinical and research laboratories. The enzymatic action of trypsin is commonly referred to as trypsinogen proteolysis or trypsinization, and proteins that have been digested or treated with trypsin are said to have been trypsinized. Trypsin was discovered in 1876 by Wilhelm Kühne. Many sources incorrectly claim that Kühne derived the name trypsin from the Ancient Greek word for rubbing, tripsis, because the enzyme was first isolated by rubbing the pancreas with glass powder and alcohol; in fact Kühne named trypsin from the Ancient Greek word thrýpto, meaning "I break" or "I break apart".