Phosphorylase activity of primary rat liver cancer.

Abstract

THE level of glycogen in the majority of tumours is considerably lower than in the normal homologous tissues1. According to Dickens and Weil-Malherbe2 the glycogen content of primary rat hepatoma is lower than that of normal rat liver. As found recently by Garanson et al. 3, the phosphorylase activity of a transplantable rat hepatoma is very low. According to these authors, the addition of adenosine 5-phosphate greatly increases the phosphorylase activity of hepatoma tissue, up to the values found with normal rat liver. Hence the low content of glycogen in hepatoma might be due to a lack of adenosine 5-phosphate, rather than a deficiency in the amount of the phosphorylase itself. On the other hand, Le Page5 found that rat hepatoma contains approximately twice as much adenosine 5-phosphate as normal rat liver. We have therefore studied the phosphorylase activity of primary rat liver carcinoma and the activating effect of adenosine 5-phosphate on it.