Electrophoretic heterogeneity of 5-phosphoribosyl-1-pyrophosphate synthetase within and among humans
- PMID: 217337
- DOI: 10.1007/BF00483742
Electrophoretic heterogeneity of 5-phosphoribosyl-1-pyrophosphate synthetase within and among humans
Abstract
The product of the enzyme 5-phosphoribosyl-1-pyrophosphate (PPriboseP) synthetase is a substrate for purine, pyrimidine, and pyridine biosynthesis and may be rate limiting for purine biosynthesis. A system developed to electrophoretically separate and histochemically detect PPriboseP synthetase in crude cell extracts has facilitated the identification of electrophoretically variant enzyme forms in the erythrocytes of five patients from a patient population of 200. Additional studies of human organs obtained at autopsy revealed a unique electrophoretic mobility for nearly each organ within the same individual.
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