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Human Hypoxanthine-Guanine Phosphoribosyltransferase (HGPRT): Purification and Properties

  • W. J. Arnold
  • R. V. LambIII
  • W. N. Kelley
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 41A)

Abstract

Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (E.C. 2.4.2.8.) catalyzes the formation of guanosine-5’-monophosphate and inosine-5’-monophosphate from 5’-phosphoribosyl-l-pyrophosphate (PPribose-P) and the purine bases guanine and hypoxanthine, respectively. Although originally assigned simply a “salvage” function in purine metabolism, the discovery of a virtually complete, X-linked deficiency of HGPRT associated with hyperuricemia, hyperuricaciduria and a bizarre neurologic syndrome (Lesch-Nyhan syndrome) has led to a reevaluation of the importance of HGPRT in the regulation of purine metabolism and central nervous system function (Seegmiller, Rosenbloom and Kelley, 1967). Therefore, an analysis of the structure of the normal enzyme is necessary to provide a basis for understanding the genetic lesion(s) producing altered or absent enzyme function. We have purified HGPRT to homogeneity from non-pooled, human male erythrocytes and have attempted to elucidate the nature of the electrophoretic heterogeneity of HGPRT activity observed during the purification (Arnold and Kelley, 1971; Kelley and Arnold, 1973).

Keywords

Central Nervous System Function Hypoxanthine Phosphoribosyltransferases Central Nervous System Dysfunction Major Protein Band Electrophoretic Variant 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Plenum Press, New York 1974

Authors and Affiliations

  • W. J. Arnold
    • 1
  • R. V. LambIII
    • 1
  • W. N. Kelley
    • 1
  1. 1.Department of MedicineDuke University Medical CenterDurhamUSA

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