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Human Adenine Phosphoribosyltransferase: Purification, Subunit Structure and Substrate Specificity

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

Abstract

Adenine phosphoribosyltransferase (APRT) catalyzes the magnesium dependent conversion of adenine to adenosine 5’-monophosphate (AMP) utilizing the high energy compound, 5-phosphoribosyl-lpyrophosphate (PP-ribose-P) as a cosubstrate. In humans this enzyme provides the only apparent pathway for conversion of dietary adenine into utilizable nucleotides. The finding of elevated levels of APRT activity in patients with the Lesch-Nyhan syndrome (Seegmiller, Rosenbloom and Kelley, 1967; Kelley, 1968) and the discovery of at least three families with a genetically determined partial deficiency of APRI activity in circulating erythrocytes (Kelley, et al., 1968; Kelley, Fox and Wyngaarden, 1970; Emmerson, et al., present symposium) stimulated our study of a highly purified preparation of human adenine phosphoribosyltransferase.

Keywords

Subunit Structure Ehrlich Ascites Tumor Cell Ehrlich Ascites Tumor Purify Enzyme Preparation Adenine Phosphoribosyltransferase 
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

  • C. B. Thomas
    • 1
  • W. J. Arnold
    • 1
  • W. N. Kelley
    • 1
  1. 1.Department of MedicineDuke University Medical CenterDurhamUSA

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