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Immunoadsorbent Chromatography of Hypoxanthine-Guanine Phosphoribosyltransferase

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

Abstract

Recent evidence indicates that the virtual absence of hypoxanthine-guanine phosphoribosyltransferase (HGPRT) in patients with the Lesch-Nyhan syndrome is due in most if not all instances to a mutation(s) on the gene coding for the HGPRT protein (Kelley and Meade, 1971; Rubin, et al., 1971; Arnold, Meade and Kelley, 1972). This mutation(s) results in the synthesis of a normal amount of a catalytically defective yet immunoreactive HGPRT enzyme protein. We have purified normal human HGPRT from erythrocytes and have prepared a highly specific antiserum in rabbits (anti-HGPRT) which displays a single precipitin line on immunodiffusion and immunoelectrophoresis with both normal hemolysate and hemolysate from patients with the Lesch-Nyhan syndrome. We have succeeded in coupling a partially-purified preparation of anti-HGPRT to cyanogen bromide activated sepharose and will present data which indicates that this technique is a promising method for the rapid isolation of both normal and mutant HGPRT.

Keywords

Cyanogen Bromide Coupling Step Chinese Hamster Fibroblast Calculated Binding Capacity HGPRT Activity 
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

© Springer Science+Business Media New York 1974

Authors and Affiliations

  • W. J. Arnold
    • 1
  • R. B. Jones
    • 1
  • W. N. Kelley
    • 1
  1. 1.Duke University Medical CenterDurhamUSA

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