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Gel filtration and velocity sedimentation in sucrose gradients were used to determine the molecular weights of purified rat renal phosphate-dependent glutaminase. The purified glutaminase has a molecular weight of 160,000 in Tris or barbital buffers and forms dimers of 332,000 molecular weight in the presence of its activator, Pi. The correlation between(More)
Rat kidney contains two distinct glutaminase isoenzymes. One requires phosphate for activity; the other is phosphateindependent but is activated 15-fold by maleate. By taking advantage of differences in activators and pH optima, specific assays were devised for each isoenzyme. Their distribution was then examined in individual structures of nephrons(More)
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