Determination of the subunit molecular weight of hypoxanthine-guanine phosphoribosyltransferase from human erythrocytes by recovery of enzyme activity from sodium dodecyl sulphate gels.
The molecular weights of the subunits of the enzyme hypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8) from human erythrocytes were determined with a simple novel method, including electrophoresis in sodium dodecyl sulphate gels, gel slicing, elution of protein from the gel slices and enzyme reactivation in the presence of the substrate 5-phosphorylribose-1-pyrophosphate. As molecular weight standards glutaraldehyde-polymerized polypeptides of human haemoglobin were used. The experiments clearly showed the existence of molecular weight differences in human erythrocyte hypoxanthine-quanine phosphoribosyltransferase.
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007041:Hypoxanthine Phosphoribosyltransferase / Q000097:blood*; D046911:Macromolecular Substances; D008970:Molecular Weight; D012967:Sodium Dodecyl Sulfate
D046911:Macromolecular Substances; D012967:Sodium Dodecyl Sulfate; D007041:Hypoxanthine Phosphoribosyltransferase