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- W2009249336 abstract "Abstract To obtain information on the tissue origin of serum amylase, partially purified preparations of rat liver and serum amylase and extracts of various tissues were subjected to cellulose acetate electrophoresis followed by detection of the amylolytic activity of starch-agar plates. A method is described for the 600-fold purification of detergent-solubilised liver amylase. The pancrease showed three bands of amylase activity migrating towards the cathode, while the parotid gland revealed five to six anodic bands. In adults rats, the serum and urine showed isoamylase patterns which were the same as those of the liver, and similar to those of the parotid. Isoamylases of the pancreatic type appeared in the serum and urine only after ligation of the commone bile duct. In newborn rats, the serum and liver contained isoamylases of the pancreatic as well as parotid type but the pancreatic type disappeard from both serum and liver by the third day after birth. There was a 100-fold increase in the levels of parotid gland amylase after weaning, which was not reflected in the levels of serum amylase. These results support the view that the liver is the major source of serum amylase in the normal rat." @default.
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- W2009249336 title "The origin of serum amylase electrophoretic studies of isoamylases of the serum, liver and other tissues of adult and infant rats" @default.
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- W2009249336 doi "https://doi.org/10.1016/0304-4165(71)90248-0" @default.
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