Abstract
The method of isoelectric focusing in polyacrylamide gel was used to separate HGPRT isoenzymes in crude hemolysates of human and rat erythrocytes. HGPRT from erythrocytes of a normal human male donor consistently revealed three peaks of activity. Their mean isoelectric points, using pH 5–7 range ampholytes, were, peak I, pI 6.00; peak II, pI 5.83; and peak III, pI 5.71. Peak III was wide and tailed. It always had a shoulder with a mean pI of 5.62. HGPRT from rat erythrocytes revealed two peaks of activity, corresponding to isoelectric points of 5.90 and 5.80. The method of isoelectric focusing in polyacrylamide gel is presented as a new way of detecting isoenzyme patterns.
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