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Complete Deficiency of Adenine Phosphoribosyltransferase

New England Journal of Medicine, 1977
We studied the clinical and biochemical manifestations of complete adenine phosphoribosyltransferase deficiency in the kindred of a male homozygous child excreting stones of 2,8-dihydroxyade-nine. Abnormal amounts of adenine, 8-hydroxyade-nine and 2,8-dihydroxyadenine (25 per cent of total purine metabolites) appeared in the urine of the propositus and
K J, Van Acker   +3 more
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Hysteretic characteristic of adenine phosphoribosyltransferase

Biochemistry, 1975
Preassay-incubation of the highly purified human erythrocyte adenine phosphoribosyltransferase (EC 2.4.2.7) (AMP pyrophosphorylase) with one of its substrates, 5-phosphoribosyl 1-pyrophosphate (PRibPP), changes the apparent V max value of the enzyme reaction.
L C, Yip, M E, Balis
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Adenine Phosphoribosyltransferase Deficiency in Iceland

Acta Medica Scandinavica, 1988
Abstract. Two children and two adults of four unrelated families were on regular light microscopic examination found to exhibit identical, spherical urine crystals. Their characteristic appearance led to the diagnosis of 2,8‐dihydroxyadenine crystalluria by spectrophotometric or gas‐chromatographic/mass‐spectrometric analysis.
T, Laxdal, T A, Jónasson
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Adenine phosphoribosyltransferase deficiency in children

Pediatric Nephrology, 2012
Adenine phosphoribosyltransferase (APRT) deficiency is a rare autosomal recessive disorder characterized by 2,8-dihydroxyadenine (2,8-DHA) crystalluria that can cause nephrolithiasis and chronic kidney disease. The aim of our study was to assess the clinical presentation, diagnosis, and outcome of APRT deficiency in a large pediatric cohort.
Jérôme, Harambat   +4 more
openaire   +2 more sources

[77] Adenine phosphoribosyltransferase

1978
Publisher Summary This chapter describes the assay method of adenine phosphoribosyltransferase (APRT) enzyme. Human APRT catalyzes the magnesium-dependent transfer of the ribose-5-phosphate moiety of 5-phosphoribosyl-l-pyrophosphate (PP-ribose-P) to the 9 position of the purine base adenine to form adenosine-5'-monophosphate (AMP).
William J. Arnold, William N. Kelley
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Studies of the binding of adenine to adenine phosphoribosyltransferase

Canadian Journal of Biochemistry, 1970
The groups on adenine phosphoribosyltransferase and on adenine which are involved in the binding of this substrate were investigated by comparing the inhibition constant of adenine with those obtained for analogues of adenine, by determining the effect of pH on the Michaelis constant of adenine, and by protection by adenine against enzyme inactivation
R E, Gadd, J F, Henderson
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A spectrophotometric assay for adenine phosphoribosyltransferase

Analytical Biochemistry, 1977
Abstract The present paper describes a new spectrophotometric assay for adenine phosphoribosyltransferase activity which is highly reproducible, rapid, sensitive, and simpler than the isotopic assays for this enzyme. This assay is based on the quantitative measurement of the product AMP by a NADH-coupled enzyme method.
SALERNO, Costantino   +1 more
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Adenine Phosphoribosyltransferase-Deficient Leishmania Donovani

1986
Mutant promastigotes of Leishmania donovani deficient in adenine phosphoribosyltransferase (APRTase) have been isolated in medium containing 4-aminopyrazolopyrimidine. The generation of APRTase-deficient mutants occurred in two discrete steps. In the first step, clones were isolated with 50% of wildtype levels of APRTase activity.
K, Kaur, D M, Iovannisci, B, Ullman
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