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Human and Mouse Hypoxanthine-Guanine Phosphoribosyltransferase: Dimers and Tetramers

Science, 1979
Human and mouse hypoxanthine-guanine phosphoribosyltransferase subunits combine to form an active heteropolymer. Dimers form the basic subunit structure of the enzymes, yet the dimers can readily associate to form tetramers. The equilibrium between dimers and tetramers is significantly influenced by the ionic strength of the enzyme solvent.
Gerald G. Johnson   +2 more
openaire   +3 more sources

Role of Human Hypoxanthine Guanine Phosphoribosyltransferase in Nucleotide Interconversion

1980
It is well established that human Hypoxanthine-Guanine Phospho-ribosyltransferase (HGPRT, EC 2.4.2.8) catalyzes the reactions: Open image in new window Open image in new ...
GIACOMELLO, Alessandro   +1 more
openaire   +4 more sources

Hypoxanthine–guanine phosphoribosyltransferase: further evidence for the identity of the binding sites for hypoxanthine and guanine

Canadian Journal of Biochemistry, 1969
Isotope exchange between hypoxanthine and both inosinate and guanylate, and between guanine and the same two ribonucleotides, support the view that hypoxanthine and guanine bind to the same site on hypoxanthine-guanine phosphoribosyltransferase.
openaire   +3 more sources

Xanthine phosphoribosyltransferase in man: Relationship to hypoxanthine-guanine phosphoribosyltransferase

Biochemical and Biophysical Research Communications, 1967
J. Frank Henderson   +3 more
openaire   +3 more sources

Genetic heterogeneity at the locus for hypoxanthine-guanine phosphoribosyltransferase.

Ciba Foundation symposium, 1977
The purine phosphoribosyltransferases have emerged as important enzymes in the metabolic economy of the developing human. Hypoxanthine-guanine phosphoribosyltransferase (HGPRT, EC 2.4.2.8) catalyses the conversion of hypoxanthine and guinine into their respective nucleotides.
openaire   +2 more sources

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