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Sandbox 50
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<applet load='1QLQ' size='300' frame='true' align='right' caption='Insert caption here' /> | <applet load='1QLQ' size='300' frame='true' align='right' caption='Insert caption here' /> | ||
=Trypsin= | =Trypsin= | ||
| - | Trypsin is a medium sized, globular, digestive serine protease that is synthesized by the pancreas and secreted into the duodenum of the small intestine. Trypsin hydrolyzes peptide bonds based on side chain specificities of the amino acids surrounding the bond to be cleaved. Trypsin's specificity is for the positively charged side chains of lysine and arginine. | + | <ref>Trypsin is a medium sized, globular, digestive serine protease that is synthesized by the pancreas and secreted into the duodenum of the small intestine.<ref/> Trypsin hydrolyzes peptide bonds based on side chain specificities of the amino acids surrounding the bond to be cleaved. Trypsin's specificity is for the positively charged side chains of lysine and arginine. |
Trypsin was first named by Kuhne in 1876, when discovered trypsin differed from pepsin in its proteolytic activity at different optimal pHs. The optimal pH for trypsin is 7.5-8.5. In 1974, trypsin's three dimensional strucutre was determined, and in the late 1980s and early 1990s, site-directed mutagenesis was performed on recombinant trypsin to determine the role of specific amino acids. | Trypsin was first named by Kuhne in 1876, when discovered trypsin differed from pepsin in its proteolytic activity at different optimal pHs. The optimal pH for trypsin is 7.5-8.5. In 1974, trypsin's three dimensional strucutre was determined, and in the late 1980s and early 1990s, site-directed mutagenesis was performed on recombinant trypsin to determine the role of specific amino acids. | ||
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===When Control Fails=== | ===When Control Fails=== | ||
When the balance between trypsin and its inhibitors, or of the activation of trypsin from trypsinogen is disturbed, pancreatitis can result. When trypsinogen is converted to trypsin early (i.e. in the pancrease), it causes the autodigestion of the pancreas. Those with cystic fibrosis often suffer from pancreatitis because it is thought that cystic fibrosis interferes with the negative feedback loop that regulates pancreatic trypsinogen secretions. When there is a high concentration of trypsin in the duodenum, a signal is sent back to the pancrease to reduce the production of trypsinogen. A high concentration of inhibitors induces pancreatic trypsinogen secretion. | When the balance between trypsin and its inhibitors, or of the activation of trypsin from trypsinogen is disturbed, pancreatitis can result. When trypsinogen is converted to trypsin early (i.e. in the pancrease), it causes the autodigestion of the pancreas. Those with cystic fibrosis often suffer from pancreatitis because it is thought that cystic fibrosis interferes with the negative feedback loop that regulates pancreatic trypsinogen secretions. When there is a high concentration of trypsin in the duodenum, a signal is sent back to the pancrease to reduce the production of trypsinogen. A high concentration of inhibitors induces pancreatic trypsinogen secretion. | ||
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| + | ==References== | ||
| + | <references/> | ||
Revision as of 03:17, 30 October 2010
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
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