[{"from": "human", "value": "Provide a description of this molecule. [C][Branch2][Ring1][Branch1][C][Branch1][P][C][Branch1][=N][C][Branch1][=Branch2][C][Branch1][Branch1][C][Ring1][=Branch1][Cl][Cl][Cl][Cl][Cl][Cl]"}, {"from": "gpt", "value": "The molecule is a potent enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds, and dairy products.  Studies on gastric digestion from 1820-1840 led to the discovery of pepsin as the substance which, in the presence of stomach acid, causes nutrients including meat or coagulated egg whites to dissolve. Soon afterward, it was shown that these protein nutrients were cleaved by pepsin to products called peptones.  Pepsin is often used as a replacement enzyme for those with pancreatic insufficiency. Stimulation of the pancreas and therefore enzymatic digestion of food is a tightly controlled and is a hormonally mediated process. Any changes or conditions affecting metabolic steps for successful digestion and absorption negatively affect pancreatic enzymatic secretion, entry into the intestine, functionality once inside the intestine, and appropriate mixing with foods/nutrients. Many causes of pancreatic insufficiency require that enzyme replacement therapy is started, including cystic fibrosis, pancreatic cancer, acute and chronic pancreatitis, as well as pancreatic surgery.  Pepsin is approved by the FDA and is used in food at levels not to exceed current good manufacturing practice. Interestingly, it has been used as a marker for laryngopharyngeal reflux (LPR), which is a common illness of otolaryngology (ear, nose and throat specialist) visits.  Interestingly, recent research has suggested that pepsin participates in the digestion of nucleic acids."}]