Abstract
This chapter discusses the amylase activity of the unstimulated rat parotid gland and rate of amylase resynthesis in the post-secretion period. The chapter presents some experiments that were designed to find out how the predominating secretory protein is synthesized in the parotid gland under catabolic conditions. Amylase was purified on the basis of its binding to starch. The radioactivity of the purified enzyme was measured by liquid scintillation counting. The weight and nitrogen content of the parotid gland were decreased under the effect of cortisone. The constancy of the amylase activity calculated for protein content suggested that the amylase activity changed parallel with the weight of the gland. The amylase activity in the parotid gland of cortisone-treated rats was enhanced markedly 15 hours after pilocarpine stimulation as compared to the same value of rats without cortisone treatment.
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