• Facets (new session)
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  • owl:sameAs
  • Inference Rule: b3sb3sifpdbprdf-labelfacetshttp://dbpedia.org/resource/inference/rules/dbpedia#http://dbpedia.org/resource/inference/rules/opencyc#http://dbpedia.org/resource/inference/rules/umbel#http://dbpedia.org/resource/inference/rules/yago#http://dbpedia.org/schema/property_rules#http://www.ontologyportal.org/inference/rules/SUMO#http://www.ontologyportal.org/inference/rules/WordNet#http://www.w3.org/2002/07/owl#ldpoplwebskos-transvirtrdf-labelNone
    

Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting these long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins. Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin was discovered in 1876 by Wilhelm Kühne