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Hypoxanthine transport in normal and hypoxanthine guanine phosphoribosyltransferase (HGPRT) deficient diploid human lymphoblasts

Experimental Cell Research, 1977
Abstract We have examined the possible relation between hypoxanthine guanine phosphoribosyltransferase (EC 2.4.2.7., HGPRT) activity and hypoxanthine transport in the normal human lymphoblast line MGL8 and two HGPRT- mutant lines derived from it. The mutant line MGL8A29 (L8A29) had considerable amounts of material cross-reacting immunologically to ...
J, Epstein, J W, Littlefield
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Hypoxanthine-guanine phosphoribosyl transferase deficiency

Human Genetics, 1976
In man congential lack of enzyme of the purine salvage system, hypoxanthineguanine phosphoribosyl transferase (HG-PRT E.C. 2.4.2.8), is mostly accompanied by a picture known as the Lesch-Nyhan snydrome. The degree of deficiency may vary from zero to a few percent of normal activity but a correlation between the severity of HG-PRT deficiency and the ...
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Electrochemical oxidation of hypoxanthine

Journal of Electroanalytical Chemistry and Interfacial Electrochemistry, 1981
Abstract The electrochemical oxidation of hypoxanthine (6-oxypurine) in aqueous solution has been studied. The evidence strongly supports the view that hypoxanthine is initially electrooxidized in a 2 e −2H + reaction to give 6,8-dioxypurine. The latter compound is more easily oxidized than hypoxanthine and is immediately further electrooxidized to ...
Arnold C. Conway   +2 more
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Hypoxanthine Transport Through Human Erythrocyte Membranes

1986
It is well known that purine bases can be taken up and utilized by the cells in nucleotide synthesis (1). In bacterial cells, purine bases from external medium are phosphoribosylated and transported through the plasma membrane in one step catalyzed by phosphoribosyltransferases which are located in the pericytoplasmic compartment (2).
CAPUOZZO, Elisabetta   +3 more
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Hypoxanthine transport in human erythrocytes

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1967
Abstract Using rapid sampling by filtration, it has been possible to follow and describe the transport of hypoxanthine across the human red blood cell membrane. The dependence of the transport rate upon the concentration of hypoxanthine is complex, and suggests a two-component mechanism. The first is a “saturable carrier system” with a K m of 0.
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Ribosyl derivatives of hypoxanthine

The Journal of Organic Chemistry, 1969
J A, Montgomery, H J, Thomas
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Structure of hypoxanthine

Acta Crystallographica Section C Crystal Structure Communications, 1988
H. W. Schmalle, G. Hänggi, E. Dubler
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