Purine Metabolism in Man—II

1. Front Matter

   Pages i-xxii

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2. History of Gout

   1. History of Gout

      • Andre de Vries

      Pages 1-12

3. Metabolic Pathways of Purines

   1. De Novo Synthesis: Precursors and Regulation

      1. A Multienzyme Complex for De Novo Purine Biosynthesis

         • Peter B. Rowe, Gemma Madsen, E. McCairns, Dorit Sauer

         Pages 13-18

      2. Coordinate Regulation of the Proximal and Distal Steps of the Pathway of Purine Synthesis De Novo in WI-L2 Human Lymphoblasts

         • Michael S. Hershfield, J. Edwin Seegmiller

         Pages 19-29

      3. Purine Toxicity in Human Lymphoblasts

         • Floyd F. Snyder, Michael S. Hershfield, J. Edwin Seegmiller

         Pages 30-39

      4. Studies on the Regulation of the Biosynthesis of Myocardial Adenine Nucleotides

         • H.-G. Zimmer, E. Gerlach

         Pages 40-49

      5. Effect of Triiodothyronine on the Biosynthesis of Adenine Nucleotides and Proteins in the Rat Heart

         • H.-G. Zimmer, G. Steinkopff, E. Gerlach

         Pages 50-58

      6. Altered Synthesis and Catabolism of Purine Nucleotides in Regulatory Mutants of <u>Saccharomyces Cerevisiae</u>

         • J. Frank Henderson, P. W. Burridge, R. A. Woods

         Pages 59-63

   2. De Novo Synthesis: Phosphoribosylpyrophosphate and Phosphoribosylpyrophosphate Synthetase

      1. Phosphoribosylpyrophosphate Synthesis in Human Erythrocytes: Inhibition by Purine Nucleosides

         • Guy Planet, Irving H. Fox

         Pages 64-70

      2. Human Phosphoribosylpyrophosphate Synthetase: Relation of Activity and Quaternary Structure

         • Michael A. Becker, Laurence J. Meyer, William H. Huisman, Cheri S. Lazar, William B. Adams

         Pages 71-79

      3. Transfer of Resistance to Selective Conditions from Fibroblasts with Mutant Feedback-Resistant Phosphoribosylpyrophosphate Synthetase to Normal Cells

         • E. Zoref, A. de Vries, O. Sperling

         Pages 80-84

      4. Phosphoribosylpyrophosphate Degradation in Human Tissues

         • Irving H. Fox, Pamela J. Marchant

         Pages 85-91

   3. De Novo Synthesis: Phosphoribosylpyrophosphate Amidotransferase

      1. Properties of the Phosphoribosylpyrophosphate-Glutamine Amidotransferase of the Human Leucemic Cells

         • H. Becher, W. Gerok

         Pages 92-98

      2. A Purine Auxotroph Deficient in Phosphoribosylpyrophosphate Amidotransferase and Phosphoribosylpyrophosphate Aminotransferase Activities with Normal Activity of Ribose-5-phosphate Aminotransferase

         • E. W. Holmes, G. L. King, A. Leyva, S. C. Singer

         Pages 99-109

   4. Nucleotide Metabolism

      1. Biochemical Studies of Purine Auxotrophs of <u>Drosophila Melanogaster</u>

         • Merrie M. Johnson, David Nash, J. Frank Henderson

         Pages 110-114

      2. Inosine Triphosphate Metabolism in Human Erythrocytes

         • J. Frank Henderson

         Pages 115-120

      3. Oxypurine and 6-Thiopurine Nucleoside Triphosphate Formation in Human Erythrocytes

         • Donald J. Nelson, Christoper Buggé, Harvey C. Krasny

         Pages 121-128

   5. Salvage Pathway

      1. Activity of the Salvage-Pathway in Erythrocytes of Newborn Infants, Children and Adults

         • M. M. Müller, P. Wagenbichler

         Pages 129-138

      2. Purine Phosphoribosyl Transferases in Human Erythrocyte Ghosts

         • C. H. M. M. de Bruyn, T. L. Oei

         Pages 139-152

      3. The Localisation of the Purine-Phosphoribosyltransferase in Rat Liver Organells

         • G. Partsch, I. Sandtner, R. Eberl

         Pages 153-156

The study of gouty arthritis has provided a common meeting ground for the research interests of both the basic scientist and the clinician. The interest of the chemist in gout began 1776 with the isolation of uric acid from a concretion of the urinary tract by the Swedish chemist SCHEELE. The same substance was subsequently extracted from a gouty tophus by the British chemist WOLLASTONE in 1797 and a half century later the cause of the deposits of sodium urate in such tophi was traced to a hyperuricemia in the serum of gouty patients by the British physician Alfred Baring GARROD who had also received training in the chemical laboratory and was therefore a fore-runner of many of today's clinician-investigators. The recent surge of progress in understanding of some of the causes of gout in terms of specific enzyme defects marks the entrance of the biochemist into this field of investigation. The identification of the first primary defect of purine metabolism associated with over-production of uric acid, a severe or partial deficiency of the enzyme hypoxanthine-guanine phospho­ ribosyltransferase was achieved less than a decade ago. The knowledge of the mechanism of purine over-production that it generated led shortly to the identification of families carrying a dominantly (possibly X-linked) inherited increase in the activity of the enzyme phosphoribosylpyrophosphate synthetase as a cause of purine over-production. Yet this is only a start as these two types of enzyme defects account for less than five per cent of gouty patients.

• Fructose
• Glutamin
• Lipid
• NADP
• Nucleotide
• Purine
• Pyrimidine
• carbohydrates
• enzyme
• enzymes
• metabolism
• mutation
• pharmacology
• protein
• synthesis

• University of Vienna, Vienna, Austria

  Mathias M. Müller, Erich Kaiser

• University of California, San Diego, La Jolla, USA

  J. Edwin Seegmiller

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