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Acute pancreatitis. Acute pancreatitis (AP) is a sudden inflammation of the pancreas. Causes, in order of frequency, include: a gallstone impacted in the common bile duct beyond the point where the pancreatic duct joins it; heavy alcohol use; systemic disease; trauma; and, in children, mumps. Acute pancreatitis may be a single event; it may be ...
Ranson criteria. Purpose. assess mortality risk of acute pancreatitis. The Ranson criteria form a clinical prediction rule for predicting the prognosis and mortality risk of acute pancreatitis. They were introduced in 1974 by the English - American pancreatic expert and surgeon Dr. John Ranson (1938–1995). [1]
Smoking increases the risk of both acute and chronic pancreatitis. [3] [4] Diagnosis of acute pancreatitis is based on a threefold increase in the blood of either amylase or lipase. [1] In chronic pancreatitis, these tests may be normal. [1] Medical imaging such as ultrasound and CT scan may also be useful. [1] Acute pancreatitis is usually ...
The most common pancreatic disease is pancreatitis, an inflammation of the pancreas which could come in acute or chronic form. Other pancreatic diseases include diabetes mellitus, exocrine pancreatic insufficiency, cystic fibrosis, pseudocysts, cysts, congenital malformations, tumors including pancreatic cancer, and hemosuccus pancreaticus.
Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site ...
Chronic pancreatitis. Chronic pancreatitis is a long-standing inflammation of the pancreas that alters the organ's normal structure and functions. [1] It can present as episodes of acute inflammation in a previously injured pancreas, or as chronic damage with persistent pain or malabsorption. It is a disease process characterized by ...
α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2] It is the major form of amylase found in humans and other mammals. [3]
An inhibitor of alpha-amylase, called phaseolamin, has been tested as a potential diet aid. [10] When used as a food additive, amylase has E number E1100, and may be derived from pig pancreas or mold fungi. Bacilliary amylase is also used in clothing and dishwasher detergents to dissolve starches from fabrics and dishes.