Abstract
Homogenates of livers from normally fed or fasted rats were fractionated by differential and density gradient centrifugation and other treatments and the distribution of α-amylase (α-1,4-glucan 4-glucanohydrolase, EC 3.2.1.1) activity among the various subcellular and submicrosomal fractions was determined. The major part of the amylase activity was found in the rough and smooth microsomal fractions. Some of this was adsorbed to the microsomes, but most became soluble only after sonication, thus supporting the view that liver amylase is a secretory protein. Fasting of the animals reduced the total amylase activity and that associated with glycogen, but increased the activity in the postmicrosomal supernatant.
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