Abstract
The activity of hypoxanthine phosphoribosyltransferase, an enzyme of purine salvage, has been measured in ten normal tissues of the rat, in regenerating liver, in developing liver, in starved and glucocorticoid-treated rats, and in several Morris hepatomas. A new method was employed, making a multiple-time-point assay practicable. Liver contained the highest activity of those tissues assayed; activity was maximum in this tissue at 32 days after birth. No correlation of enzyme activity with tissue growth rate was apparent. Kinetic studies on the enzymes from normal liver and Morris hepatoma 3924A indicated half-maximal velocities were attained at concentrations of about 4 μM hypoxanthine, and about 5 μM phosphoribosylpyrophosphate.
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