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. 1978 Oct;16(9-10):905-16.
doi: 10.1007/BF00483742.

Electrophoretic heterogeneity of 5-phosphoribosyl-1-pyrophosphate synthetase within and among humans

R V Lebo, D W Martin Jr

Electrophoretic heterogeneity of 5-phosphoribosyl-1-pyrophosphate synthetase within and among humans

R V Lebo et al. Biochem Genet. 1978 Oct.

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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