Results 191 to 200 of about 37,163 (226)
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1974
Partial deficiency of HGPRT, a salvage enzyme of purine metabolism, has been demonstrated to be the primary abnormality causing purine overproduction in a small proportion of patients with gout (1–4). The quantitative deviation in the activity of this enzyme has been shown by Kelley et al.
O, Sperling, P, Boer, A, De Vries
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Partial deficiency of HGPRT, a salvage enzyme of purine metabolism, has been demonstrated to be the primary abnormality causing purine overproduction in a small proportion of patients with gout (1–4). The quantitative deviation in the activity of this enzyme has been shown by Kelley et al.
O, Sperling, P, Boer, A, De Vries
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[77] Adenine phosphoribosyltransferase
1978Publisher Summary This chapter describes the assay method of adenine phosphoribosyltransferase (APRT) enzyme. Human APRT catalyzes the magnesium-dependent transfer of the ribose-5-phosphate moiety of 5-phosphoribosyl-l-pyrophosphate (PP-ribose-P) to the 9 position of the purine base adenine to form adenosine-5'-monophosphate (AMP).
William J. Arnold, William N. Kelley
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Biochemical and Biophysical Research Communications, 1967
W N, Kelley +3 more
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W N, Kelley +3 more
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[Adenine phosphoribosyltransferase (APRT)].
Nihon rinsho. Japanese journal of clinical medicine, 1997Adenine phosphoribosyltransferase (APRT) is a purine metabolic enzyme that salvages adenine moiety generated via the polyamine synthetic pathway. Adenine is produced by the cleavage of methylthiodenosine (MTA), a by-product of the polyamine synthesis.
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Quinolinate phosphoribosyltransferase
Biochemical and Biophysical Research Communications, 1965Paul M. Packman, William B. Jakoby
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Dioxotetrahydropyrimidine phosphoribosyltransferase
1996Dietmar Schomburg, Dörte Stephan
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