Purification and characterization of mouse 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...
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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...
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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 کاملHuman hypoxanthine-guanine phosphoribosyltransferase. Purification and characterization of mutant forms of the enzyme.
Erythrocyte hypoxanthine-guanine phosphoribosyltransferase has been highly purified from five unrelated patients with a deficiency of this enzyme. Affinity chromatography using either GMP-Sepharose or an immunoadsorbent was the most productive step in the purifications. The specific activity of the purified enzyme was unchanged for patients L. P. and G. S., and slightly decreased for patient R....
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: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41989-3