Chymotrypsinogen: Difference between revisions
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'''Chymotrypsinogen''' is a precursor ([[zymogen]]) of the [[digestive enzyme]] [[chymotrypsin]]. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the [[duodenum]].<ref>Berg.M.J.,Tymoczko.L.J.,Stryer.L., Gatto Jr. J.G. ''Biochemistry'', 7th Ed.; Freeman: New York, 2012. </ref> Chymotrypsinogen must be inactive until it gets to the digestive tract, so no damage is done to the pancreas or an other organs. It is activated into its active form by another enzyme called [[trypsin]]. This active form is called π-Chymotrypsin and is used to create α-Chymotrypsin. The [[trypsin]] cleaves the chymotrypsinogen at the arginine and isolucine peptide bond. This creates two π-chymotrypsin molecules. One of the π-chymotrypsin acts on the other by breaking a leucine and serine peptide bond. This yields the |
'''Chymotrypsinogen''' is a precursor ([[zymogen]]) of the [[digestive enzyme]] [[chymotrypsin]]. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the [[pancreas]] and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the [[duodenum]].<ref>Berg.M.J.,Tymoczko.L.J.,Stryer.L., Gatto Jr. J.G. ''Biochemistry'', 7th Ed.; Freeman: New York, 2012. </ref> Chymotrypsinogen must be inactive until it gets to the digestive tract, so no damage is done to the pancreas or an other organs. It is activated into its active form by another enzyme called [[trypsin]]. This active form is called π-Chymotrypsin and is used to create α-Chymotrypsin. The [[trypsin]] cleaves the chymotrypsinogen at the [[arginine]] and [[isolucine]] peptide bond. This creates two π-chymotrypsin molecules. One of the π-chymotrypsin acts on the other by breaking a [[leucine]] and [[serine]] peptide bond. This yields the α-chymotrypsin.<ref> Dryer.J.W.,Neurath.H. ''The Activation of Chemotyrpsinogen: ISOLATION AND IDENTIFICATION OF A PEPTIDE LIBERATED DURING ACTIVATION '' Department of Biochemistry, University of Washington [1955]http://www.jbc.org/content/217/2/527.full.pdf [accessed Oct. 10, 2012]</ref> |
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==References== |
==References== |
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Revision as of 20:37, 11 October 2012
Chymotrypsinogen is a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum.[1] Chymotrypsinogen must be inactive until it gets to the digestive tract, so no damage is done to the pancreas or an other organs. It is activated into its active form by another enzyme called trypsin. This active form is called π-Chymotrypsin and is used to create α-Chymotrypsin. The trypsin cleaves the chymotrypsinogen at the arginine and isolucine peptide bond. This creates two π-chymotrypsin molecules. One of the π-chymotrypsin acts on the other by breaking a leucine and serine peptide bond. This yields the α-chymotrypsin.[2]
References
- ^ Berg.M.J.,Tymoczko.L.J.,Stryer.L., Gatto Jr. J.G. Biochemistry, 7th Ed.; Freeman: New York, 2012.
- ^ Dryer.J.W.,Neurath.H. The Activation of Chemotyrpsinogen: ISOLATION AND IDENTIFICATION OF A PEPTIDE LIBERATED DURING ACTIVATION Department of Biochemistry, University of Washington [1955]http://www.jbc.org/content/217/2/527.full.pdf [accessed Oct. 10, 2012]
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