Abstract
Purine phosphoribosyltransferases were assayed in crude extracts of mouse liver, spleen, kidney, heart, lung, cerebrum and red cells, which also contain xanthine oxidase, guanase, 5'-nucleotidase and adenosine deaminase, by the method which was based on the isolation of the products by electro-phoresis on cellulose acetate membrane. Purine phosphoribosyltransferase activities were found in all tissues examined. Among them, the activities in the cerebrum were higher than those of other tissues whereas activities in the red cells were very low. The activity ratios of hypoxanthine-guanine phosphoribosyltransferase with hypoxanthine and guanine as the substrates to adenine phosphoribosyltransferase were 0.9-2.1 and 1.8-4.1, respectively, in the liver, spleen, heart, lung and kidney. In the cerebrum these were 7.4 and 19.2, and were 0.2 and 0.2 in the red cells. The significance of these results has been discussed.
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