Abstract
In the rat pancreas, normal diurnal and pilocarpine-induced variations in the protein, ribonuclease (RNase), and water content were studied. The results show a considerable variation in the dirunal content of RNase, whereas the protein and water concentrations remained constant. Furthermore, the experiments provide evidence that RNase is secreted by means of a mechanism partly independent of other proteins and that every zymogen granule does not contain the same amount of the enzyme. The earlier presumption that there are at least two intracellular storage forms of the enzyme is confirmed and the intracellular variability in the capacity to attract anti-RNase antibodies is explained.
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