Isolation of four components from purified human erythrocyte hypoxanthine-guanine phosphoribosyltransferase by isoelectric focusing.
Erythrocyte HGPRT from a male donor was partially purified by DEAE-cellulose chromatography and by fractionation between 35 and 65% ethanol. Isoelectric focusing of the ethanol fraction resolved HGPRT activity into four components which were numbered I-IV beginning with the one nearest the cathode. A second isoelectric focusing of component II (the most active) resulted in 94% of the activity as a single component. When mixed, however, the four components could be separated again by isoelectric focusing. The appearance of these different molecular forms of the enzyme could be due to post-transcriptional alterations or to formation of enzyme complexes.
D002848:Chromatography, DEAE-Cellulose; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007041:Hypoxanthine Phosphoribosyltransferase / Q000032:analysis / Q000097:blood*; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000032:analysis; D007926:Lesch-Nyhan Syndrome / Q000201:enzymology; D008297:Male; D014158:Transcription, Genetic
D007527:Isoenzymes; D007041:Hypoxanthine Phosphoribosyltransferase