Abstract
The intracellular distribution of amylase in rat pancreas has been studied by differential centrifugation of pancreas homogenates. Although the secretory granules showed high activity, at least half the amylase activity was recovered in the microsome and supernatant fluid fractions. In the latter fractions, the proportion of the total enzyme activity and the concentration of amylase activity relative to protein-nitrogen showed consistent variations with changes in the secretory state of the gland. Apparently some of the amylase is associated with the endoplasmic reticulum in the living pancreas cell, and during homogenization in 0.88 M sucrose.the endoplasmic reticulum is broken into pieces resembling one another in composition but differing in size. During exposure to 0.25 M sucrose some dissociation of the components of this material takes place, but when such dissociation occurs the amylase protein is not preferentially associated with either the ribonucleoprotein granules or the lipoprotein reticulum of the microsome fraction.
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