Purification and characterization of hypoxanthine-guanine phosphoribosyltransferase from Saccharomyces cerevisiae

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Abstract
Hypoxanthine-guanine phosphoribosyltransferase (HPRT) was purified 12,000-fold to homogeneity from yeast [S. cerevisiae] by a three-step procedure including acid precipitation, anion-exchange chromatography and GMP affinity chromatography. The enzyme is a dimer consisting of 2, probably identical, subunits of MW 29,500. The enzyme recognizes hypoxanthine and guanine, but not adenine or xanthine, as substrates. An antiserum against native and denatured enzyme has been raised and shown to be specific for the enzyme. The antiserum has no affinity for Chinese hamster or human HPRT but does recognize subunits of yeast HRPT as well as some cyanogen bromide fragments of the enzyme.