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....

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Bibliographic Details
Published in:Biochemical genetics 1975-04, Vol.13 (3-4), p.255-261
Main Authors: Gulumian, M, Wakid, N W
Format: Article
Language:English
Subjects:
Chromatography, DEAE-Cellulose
Erythrocytes - enzymology
Humans
Hypoxanthine Phosphoribosyltransferase - analysis
Hypoxanthine Phosphoribosyltransferase - blood
Isoelectric Focusing
Isoenzymes - analysis
Lesch-Nyhan Syndrome - enzymology
Male
Transcription, Genetic
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Summary: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.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF00486020