Developmental expression of murine HPRT. I. Activities, heat stabilities, and electrophoretic mobilities in adult tissues.

Total and specific activity of the enzyme hypoxanthine phosphoribosyltransferase (HPRT) varied widely among six tissues from C3H/f mice; the highest levels of activity were in brain. More striking were thermostability differences in tissue enzymes. Although brain, spleen, and kidney HPRT retained 65% basal activity after 15 min at 85 C, heart, liver, and erythrocyte HPRT retained only 20-30% initial activity. Kidney HPRT behaved as monospecific heat-stable enzyme (K-denatauration=0.022/min, and liver enzyme behaved as monospecific heat-labile enzyme (K-denaturation=0.061/min), while other tissues appeared to contain both forms of the enzyme. Multiple electrophoretic activity bands were present in all tissues; no activity band was restricted to a single tissue. The data presented here are consistent with the hypothesis that the distinct tissue properties of HPRT result from posttranslational modification of the product of a single genetic locus which is expressed in all tissues.