Human hypoxanthine-guanine phosphoribosyltransferase. Evidence for tetrameric structure.
Hypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8) has been purified 23,000-fold from normal human erythrocytes. The purification includes affinity chromatography on a GMP column. The subunit molecular weight of the enzyme obtained from this purification is 24,000. The finding of four protein species after cross-linkage of the highly purified enzyme with dimethylsuberimidate, dimethyladipimidate, and glutaraldehyde suggests that the enzyme may exist in the native state as a tetramer.
D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D007041:Hypoxanthine Phosphoribosyltransferase / Q000097:blood / Q000302:isolation & purification; D046911:Macromolecular Substances; D008970:Molecular Weight; D011487:Protein Conformation
D046911:Macromolecular Substances; D007041:Hypoxanthine Phosphoribosyltransferase