Some properties of erythrocyte adenine phosphoribosyltransferase in gout due to partial hypoxanthine guanine phosphoribosyltransferase deficiency

O. Sperling, P. Boer, A. De Vries

Research output: Contribution to journalArticlepeer-review

Abstract

Some properties of the erythrocyte adenine phosphoribosyltransferase (APRT) were studied in the dialyzed hemolysates of two gouty subjects with partial hypoxanthine guanine phosphoribosyltransferase (HGPRT) deficiency, whose erythrocyte APRT exhibited increased activity and thermal stability. The enzyme was found similar to that in hemolysates from normal subjects in view of Michaelis Menten constants for the substrates adenine and phosphoribosylpyrophosphate (PRPP), electrophoretic mobility on starch gel, pH profile, and sensitivity to product and feedback inhibition. The thermostability of the APRT in hemolysates of normal erythrocytes could be increased by addition of PRPP. The data is compatible with the assumption that the increased erythrocyte APRT activity and thermostability are a result of substrate stabilization due to the accumulation of PRPP in the HGPRT deficient cells and do not represent an APRT mutant.

Original languageEnglish
Pages (from-to)153-157
Number of pages5
JournalRhumatologie
Volume3
Issue number2
StatePublished - 1973

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