Results 141 to 150 of about 6,350 (165)

Purification of Adenine Phosphoribosyltransferase by Affinity Chromatography

Preparative Biochemistry, 1978
The 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.
Milton W. Taylor, Howard V. Hershey
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Purification and Characterization of Mammalian Adenine Phosphoribosyltransferases

1980
In 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.
Howard V. Hershey, Milton W. Taylor
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Severe impairment in adenine metabolism with a partial deficiency of adenine phosphoribosyltransferase

Metabolism, 1985
Among three unrelated patients with recurrent 2,8-dihydroxyadenine urolithiasis, two completely lacked adenine phosphoribosyltransferase (APRT) in both erythrocytes and proliferative T cells. The third patient possessed significant enzyme activities in both hemolysates and T-cell extracts at levels comparable to heterozygotes for complete APRT ...
Kusuki Nishioka, Kiyoshi Tatara, Kiyoko Kaneko, Fujio Takeuchi, Naoyuki Kamatani, Hisashi Yamanaka, Shin Fujimori, Yutaro Nishida, Yohei Tofuku, Ieo Akaoka   +9 more
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Mutational Basis of Adenine Phosphoribosyltransferase Deficiency

1991
The 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
Ju Chen, Jay A. Tischfield, Amrik Sahota, Peter J. Stambrook   +3 more
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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, H. A. Simmonds, J.S. Cameron, C. F. Potter   +3 more
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Adenine Phosphoribosyltransferase Deficiency in a Female with Gout

1974
A moderate deficiency of adenine phosphoribosyltransferase (APRTase) has been described in two families (1,2). In the first of these families the deficiency of APRTase extended to four members in three generations. However in these cases, there was no evidence of abnormal urate metabolism.
Bryan T. Emmerson, Ross B. Gordon, L. Thompson   +2 more
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Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase

Proteins: Structure, Function, and Genetics, 1996
Adenine phosphoribosyltransferase from the protozoan parasite Leishmania donovani has been crystallized in the presence of the substrate Mg(2+)-alpha-D-5-phosphoribosyl-1-pyrophosphate (PRPP) or the product adenosine-5-monophosphate, as well as in the absence of ligand.
Cynthia L. Phillips, Richard G. Brennan, Buddy Ullman   +2 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.
Kiran J Kaur, Buddy Ullman, David M. Iovannisci   +2 more
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Purification of adenine phosphoribosyltransferase from Brassica juncea

Archives of Biochemistry and Biophysics, 1990
Adenine 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.
Chris Somerville, Barbara A. Moffatt
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[79] Adenine phosphoribosyltransferase from rat liver

1978
Publisher Summary This chapter describes the methodology of purification of adenine phosphoribosyltransferase from rat liver. All steps in the purification are carried out at 2–4°, and all solutions contain 5 mM mercaptoethanol, unless stated otherwise.
James G. Kenimer, Donald P. Groth, Leona G. Young   +2 more
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