Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferase
نویسندگان
چکیده
منابع مشابه
Hypoxanthine-Guanine Phosphoribosyltransferase Variant
A B S T R A C T We have previously described a 14-yrold boy with hyperuricemia, renal failure, and accelerated purine production resistant in vivo and in vitro to purine analogs. This patient demonstrated normal red cell hypoxanthine-guanine phosphoribosyltransferase (HPRT) heat stability, electrophoresis at high pH, and activity at standard substrate levels. In the present report an abnormal H...
متن کاملHuman hypoxanthine-guanine phosphoribosyltransferase.
A mutant form of human hypoxanthine-guanine phosphoribosyltransferase (HPRTToronto) was isolated from erythrocytes of a male patient with gout due to a partial deficiency of enzyme activity. The tryptic peptides of HPRTToronto were mapped by reverse-phase high pressure liquid chromatography in an attempt to define the precise abnormality in its primary structure. Sequence analysis of the single...
متن کاملPlasmodium falciparum hypoxanthine guanine phosphoribosyltransferase. Stability studies on the product-activated enzyme.
Hypoxanthine guanine phosphoribosyltransferases (HGPRTs) catalyze the conversion of 6-oxopurine bases to their respective nucleotides, the phosphoribosyl group being derived from phosphoribosyl pyrophosphate. Recombinant Plasmodium falciparum HGPRT, on purification, has negligible activity, and previous reports have shown that high activities can be achieved upon incubation of recombinant enzym...
متن کاملChinese Hamster Hypoxanthine-Guanine Phosphoribosyltransferase
Hypoxanthine-guanine phosphoribosyltransferase from Chinese hamster brain, liver, and V79 tissue culture cells appears to have identical structural and catalytic properties. The enzyme has been purified 540-fold to apparent homogeneity from Chinese hamster brain. The native molecular weight is 78,000 to 85,000 determined by Sephadex G-100 column chromatography and acrylamide gel electrophoresis...
متن کاملKinetic studies of hypoxanthine-guanine phosphoribosyltransferase.
The mechanism of reaction of human erythrocyte hypoxanthine-guanine phosphoribosyltransferase was investigated by initial velocity, product inhibition, and isotope exchange studies. Although initial velocity data are compatible with a mechanism involving binary enzyme-substrate complexes, the product inhibition and isotope exchange studies indicate that the reaction is ordered with the formatio...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2005
ISSN: 1742-464X,1742-4658
DOI: 10.1111/j.1742-4658.2005.04620.x