Abstract
There are two different types of aldolase in mammalian tissues, the main difference between these isozymes is the relative activity towards the second substrate of aldolase, fructose- 1-phosphate (F- 1-P). In normal liver the ratio of the activities towards fructose di-phosphate (F-d-P) and towards fructose- 1-phosphate, is near 1, because normal liver contains almost exclusively the type of aldolase characterized by a ratio F-d-P/F-1-P= 1. In human primary liver cancer (and also in experimental hepatoma), this ratio is raised to a mean value of 5.5. On the contrary, muscle contains almost exclusively the type of aldolase with a ratio greater than 50. The two types of aldolase exist in normal spleen, but principally the latter type. In spleen of normal mice, we have found an aldolase ratio of 8.97; in experimental cancer (reticulum cell sarcoma of spleen) we have found the ratio lowered to 4·51. These results are discussed in presenting the hypothesis of the repression, in cancer, of the most differentiated enzyme.
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