Abstract
A new method is presented for the purification of human glucose-6-phosphate dehydrogenase (G6PD) using affinity chromatography with 2′5′-ADP-Sepharose 4B followed by automated ion-exchange chromatography with DEAE 5PW. This rapid method allows a high recovery of enzyme activity from even a small amount of blood; the yield is about 90% after the first purification step and 70% at the end of the procedure. There is an excellent reproducibility of the kinetic parameters and optimal biochemical characterization of G6PD is achieved even for variants associated with severe enzyme deficiency ( e.g. G6PD Mediterranean).
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