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Abstract
1. 1. Glucose-6-phosphate dehydrogenase (G6PDH) has been purified to homogeneity from rat and chick brain by affinity chromatography with Sepharose bound 2′,5′ ADP. 2. 2. Some properties of the two enzymes are studied and the effects of hydrogen ion concentration, Mg 2+ ions, temperature and urea on the initial rate of enzyme are described. 3. 3. G6PDH from chick brain differs from the rat enzyme in affinity for 2′,5′ ADP Sepharose, in pH optimum, in heat stability and it is differently affected by Mg 2+ ions. No effect is detectable after urea treatment on enzymes from both sources.
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