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Human Polyclonal APRT Primary Antibody für IHC (p), WB - ABIN389427
Valaperta, Rizzo, Lombardi, Verdelli, Piccoli, Ghiroldi, Creo, Colombo, Valisi, Margiotta, Panella, Costa: Adenine phosphoribosyltransferase (APRT) deficiency: identification of a novel nonsense mutation. in BMC nephrology 2014
LOH on nonselected chromosomes was infrequent in Aprt mutants exhibiting intragenic events or mitotic recombination for chromosome 8
Data shsow that despite continuous selection for expression of the reactivated Aprt alleles, exceptionally high spontaneous re-silencing frequencies were observed.
silencing of mouse Aprt is a gradual process in the differentiated cells
A long TA repeat in the promoter region of IL28B (zeige IL28B Antikörper) was associated with spontaneous HCV clearance.
A new mutation, p.Gln147X, in APRT gene, was found in a patient with adenine phosphoribosyltransferase deficiency.
Case study of 2 year old Japanese boy with APRT deficiency. Genetic analysis showed compound heterozygote APRT*J and missense mutation L33P. APRT deficiency should be suspected in patients with radiolucent kidney stones and urinary 2,8-DHA crystals.
kinetic, regulatory and thermostability properties of APRT from erythrocytes of HGPRT (zeige HPRT1 Antikörper) deficient patients
two novel mutations, G133D and V84M, were found in the APRT gene in Japanese patients with APRT deficiency
APRT assay in a sample of patient hemolysate showed no detectable activity of the enzyme (25.56+/-9.55 U/L red blood cells in control healthy subjects).
The phosphorylation status of membrane-bound nucleoside diphosphate kinase in epithelia and the role of AMP are reported.
Adenine phosphoribosyltransferase belongs to the purine/pyrimidine phosphoribosyltransferase family. A conserved feature of this gene is the distribution of CpG dinucleotides. This enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). It also produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in this enzyme causes 2,8-dihydroxyadenine urolithiasis. Two transcript variants encoding different isoforms have been found for this gene.
, AMP diphosphorylase
, AMP pyrophosphorylase