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Adenine phosphoribosyltransferase deficiency and renal allograft dysfunction
American Journal of Kidney Diseases, 2001Adenine phosphoribosyltransferase (APRT) deficiency is a rarely diagnosed cause of renal allograft dysfunction. We report the case of a 42-year-old man who presented in 1996 with idiopathic renal failure. Native kidney biopsy showed extensive microcrystalline interstitial nephritis.
B, Benedetto +5 more
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Inheritance of Adenine Phosphoribosyltransferase (APRT) Deficiency
1980Recognition of the importance of the enzyme hypoxanthine-guanine phosphoribosyltransferase (HGPRT) in the control of purine metabolism lead to systematic investigations of the companion purine salvage enzyme, adenine phosphoribosyltransferase (APRT). This was followed by the discovery of individuals (considered to be heterozygous for the defect) with ...
K J, Van Acker +3 more
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Purification of adenine phosphoribosyltransferase from Brassica juncea
Archives of Biochemistry and Biophysics, 1990Adenine phosphoribosyltransferase was purified from Brassica juncea leaves approximately 4000-fold, to homogeneity. The native enzyme is a homodimer, with a Mr of 54,000. The purification involved (NH4)2SO4 fractionation, differential ultracentrifugation, and anion-exchange, hydrophobic, dye-ligand, and affinity chromatography.
B A, Moffatt, C R, Somerville
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Complete Deficiency of Adenine Phosphoribosyltransferase
New England Journal of Medicine, 1977We 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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Mutational Basis of Adenine Phosphoribosyltransferase Deficiency
1991The mutational basis of APRT deficiency was studied in non-Japanese and Japanese patients. Fifteen different mutations have been identified altogether. Of these 4 were common, 6 were located in exon 3, and two at the exon 4-intron 4 junction. The common mutations were a missense mutation in exon 3 (asp65----val) and a T insertion at the exon 4-intron 4
A, Sahota +3 more
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Purification of Adenine Phosphoribosyltransferase by Affinity Chromatography
Preparative Biochemistry, 1978The purine salvage pathway enzyme adenine phosphoribosyltransferase (AMP: pyrophosphate phosphoribosyltransferase EC 2.42.7) has been purified to greater than 85% homogeneity from crude rat liver 100,000 x g supernatant in one step by affinity chromatography.
H V, Hershey, M W, Taylor
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Adenine phosphoribosyltransferase deficiency: A simple diagnostic test
Clinical Science, 19881. A simple method for diagnosing adenine phosphoribosyltransferase (APRT) deficiency using urine is described. 2. T.l.c. of 1 μl of urine from a child with APRT deficiency was performed and adenine was easily detected by its brilliant blue phosphorescence at liquid nitrogen temperature. 3.
J L, Maddocks, S A, Al-Safi
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[Adenine phosphoribosyltransferase (APRT)].
Nihon rinsho. Japanese journal of clinical medicine, 1997Adenine phosphoribosyltransferase (APRT) is a purine metabolic enzyme that salvages adenine moiety generated via the polyamine synthetic pathway. Adenine is produced by the cleavage of methylthiodenosine (MTA), a by-product of the polyamine synthesis.
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Mechanisms of inhibition of adenine phosphoribosyltransferase by adenine nucleosides and nucleotides
Canadian Journal of Biochemistry, 1970Kinetic studies of the inhibition of adenine phosphoribosyltransferase by adenine 6′-deoxyallofuranoside and 2′-deoxyadenylate indicate that both compounds bind to free enzyme and to the enzyme–phosphoribosylpyrophosphate complex, although they bind with different relative affinities to each enzyme form. The sites to which these inhibitors bind appear
J F, Henderson +3 more
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Purification and Characterization of Mammalian Adenine Phosphoribosyltransferases
1980In mammals, the enzyme adenine phosphoribosyl transferase (APRT; AMP: pyrophosphate phosphoribosyl transferase; E.C. 2·42·7) is the only known mechanism by which dietary adenine can be utilized1. In humans with reduced or absent APRT activity, renal stones containing substantial amounts of 2,8-dioxyadenine can occur1.
M W, Taylor, H V, Hershey
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