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Studies on the coordinate activity and lability of orotidylate phosphoribosyltransferase and decarboxylase in human erythrocytes, and the effects of allopurinol administration
Richard M. Fox, … , Margaret H. Wood, William J. O'Sullivan
Richard M. Fox, … , Margaret H. Wood, William J. O'Sullivan
Published May 1, 1971
Citation Information: J Clin Invest. 1971;50(5):1050-1060. https://doi.org/10.1172/JCI106576.
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Research Article

Studies on the coordinate activity and lability of orotidylate phosphoribosyltransferase and decarboxylase in human erythrocytes, and the effects of allopurinol administration

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Abstract

A coordinate relationship between the activities of two sequential enzymes in the de novo pyrimidine biosynthetic pathway has been demonstrated in human red cells. The two enzymes, orotidylate phosphoribosyltransferase and decarboxylase are responsible for the conversion of orotic acid to uridine-5′-monophosphate. Fractionation of red cells, on the basis of increase of specific gravity with cell age, has revealed that these two enzymes have a marked but equal degree of lability in the ageing red cell. It is postulated that orotidylate phosphoribosyltransferase and decarboxylase form an enzyme-enzyme complex, and that the sequential deficiency of these two enzymes in hereditary orotic aciduria may reflect a structural abnormality in this complex.

Authors

Richard M. Fox, Margaret H. Wood, William J. O'Sullivan

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