Trypsin

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Trypsin is found in the digestive system, it's a protease [[Enzyme|enzyme]] produced in the [[Pancreas|pancreas]]. Trypsin is an [[Endopeptidase|endopeptidase]]. This means that it cleaves [[Amino acids|amino acids]] in the middle of the [[Polypeptide chain|polypeptide chain]] as opposed to cleaving the amino acids on the end of the polypeptide chain. It is a hydrolytic endopeptidase as it uses [[Hydrolysis|hydrolysis]] as the mechanism to break down polypeptides.<ref name="null">Biologyguide.net, (2015). Digestive System. [online] Available at: http://www.biologyguide.net/bya7/bya7-16-4.htm [Accessed 2 Dec. 2015].</ref> Trypsin is used in some proteomic investigations where the enzyme is used to cleave the peptide in question at specific points, at the C- terminal to Arginine and&nbsp;Lysine residues.<ref>Olsen J. Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues. Molecular &amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp; Cellular Proteomics. 2004;3(6):608-614.</ref>&nbsp;The resulting peptides can be recorded in a database, this data can be used to identify this protein in future studies.<ref>What is Proteomics? [Internet]. Office of Cancer Clinical Proteomics Research - National Cancer Institute. 2016 [cited 17 October 2016]. Available from: http://proteomics.cancer.gov/whatisproteomics</ref>  
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Trypsin is found in the digestive system, it's a protease [[Enzyme|enzyme]] produced in the [[Pancreas|pancreas]]. Trypsin is an [[Endopeptidase|endopeptidase]]. This means that it cleaves [[Amino acids|amino acids]] in the middle of the [[Polypeptide chain|polypeptide chain]] as opposed to cleaving the amino acids on the end of the polypeptide chain. It is a hydrolytic endopeptidase as it uses [[Hydrolysis|hydrolysis]] as the mechanism to break down polypeptides<ref name="null">Biologyguide.net, (2015). Digestive System. [online] Available at: http://www.biologyguide.net/bya7/bya7-16-4.htm [Accessed 2 Dec. 2015].</ref>. Trypsin is used in some proteomic investigations where the enzyme is used to cleave the peptide in question at specific points, at the C- terminal to Arginine and&nbsp;Lysine residues<ref>Olsen J. Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues. Molecular &amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp; Cellular Proteomics. 2004;3(6):608-614.</ref>. The resulting peptides can be recorded in a database, this data can be used to identify this protein in future studies<ref>What is Proteomics? [Internet]. Office of Cancer Clinical Proteomics Research - National Cancer Institute. 2016 [cited 17 October 2016]. Available from: http://proteomics.cancer.gov/whatisproteomics</ref>.
  
 
=== References  ===
 
=== References  ===
  
 
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Revision as of 11:59, 17 November 2017

Trypsin is found in the digestive system, it's a protease enzyme produced in the pancreas. Trypsin is an endopeptidase. This means that it cleaves amino acids in the middle of the polypeptide chain as opposed to cleaving the amino acids on the end of the polypeptide chain. It is a hydrolytic endopeptidase as it uses hydrolysis as the mechanism to break down polypeptides[1]. Trypsin is used in some proteomic investigations where the enzyme is used to cleave the peptide in question at specific points, at the C- terminal to Arginine and Lysine residues[2]. The resulting peptides can be recorded in a database, this data can be used to identify this protein in future studies[3].

References

  1. Biologyguide.net, (2015). Digestive System. [online] Available at: http://www.biologyguide.net/bya7/bya7-16-4.htm [Accessed 2 Dec. 2015].
  2. Olsen J. Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues. Molecular &amp;amp;amp;amp;amp;amp;amp;amp;amp;amp;amp; Cellular Proteomics. 2004;3(6):608-614.
  3. What is Proteomics? [Internet]. Office of Cancer Clinical Proteomics Research - National Cancer Institute. 2016 [cited 17 October 2016]. Available from: http://proteomics.cancer.gov/whatisproteomics
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