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PubMed1975

Electrophoretic and immunological properties of liver alpha-amylase of well-fed and fasted rats.

1. Alpha-Amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) in the liver of well-fed rats showed a characteristic electrophoretic mobility between those of pancreatic and parotid amylases. Amylase in the liver of fasted rats showed an electrophoretic mobility identical to that of parotid amylase. When fasted rats were re-fed on a standard diet for two days the electrophoretic mobility of their liver amylase returned to that of the liver amylase of well-fed rats. 2. When purified rat pancreatic and parotid amylases were mixed with a final concentration of 4% glycogen solution, their electrophoretic mobilities both became similar to that of liver amylase of well-fed rats. The electrophoretic mobility of glycogen corresponded to that of liver amylase of well-fed rats. Since liver amylase of fasted rats has the same mobility as parotid amylase and serum contains only parotid-type amylase, these findings suggest that liver amylase of well-fed rats may be a complex of serum amylase and glycogen. 3. The antigenicities of the liver amylases of well-fed and fasted rats were the same as that of purified parotid amylase, but different from that of purified pancreatic amylase. Amylase in serum and urine, which had the same electrophoretic mobility as parotid amylase, had the same antigenicity as purified parotid amylase and the liver amylases of well-fed and fasted rats.

Amylases↗
PubMed1991

Lipase and pancreatic amylase activities in tissues and in patients with hyperamylasemia.

Lipase, pancreatic amylase, and total amylase activities were measured in nondiseased and diseased human pancreatic tissues and in six different locations of the human digestive system. In addition, it was determined whether serum lipase and pancreatic amylase tests could replace the total amylase test to improved diagnostic efficiency in the evaluation of acute pancreatitis in hyperamylasemia patients. Nondiseased pancreatic tissue contained 4.5 times more lipase activity than total amylase activity. Diseased pancreatic tissue contained less activity for both lipase and total amylase compared to normal tissue. The total amylase activity of the pancreas was comprised solely of pancreatic amylase. Tissue obtained from six different anatomic locations in the digestive system contained 35 to 45 times less lipase and total amylase activity compared to the pancreas. Total amylase activity of the digestive system tissues were comprised of 25% pancreatic and 75% salivary isoamylases. Lipase, pancreatic amylase, and total amylase levels also were determined in serial serum samples from 17 consecutive hyperamylasemia patients admitted with possible acute pancreatitis. The serum lipase level remained higher than normal longer than either the total amylase and pancreatic amylase levels. In patients with hyperamylasemia of pancreatic origin, a poor correlation was observed at admission between serum pancreatic amylase and serum lipase. Not all patients with elevated lipase had an elevated pancreatic amylase level and vice versa. However, in every patient pancreatic disease would have been detected by the elevation of either lipase or pancreatic amylase levels. Diagnostic efficiency for pancreatic disease using serum pancreatic amylase, lipase, and total amylase tests was 94.1%, 76.5%, and 64.7%, respectively. These data suggest that lipase and pancreatic amylase tests are specific for the pancreas and might be considered replacements for total amylase as the stat or routine laboratory test for the diagnosis of pancreatic tissue injury.

Acute Disease↗