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.