A two-step purification procedure for sheep liver 6-phosphogluconate dehydrogenase
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D O Somers1, J Hajdu, M J Adams
1Laboratory of Molecular Biophysics, University of Oxford, United Kingdom.
Protein Expression and Purification
|October 1, 1991
Abstract:
A two-step procedure for the purification of 6-phosphogluconate dehydrogenase (EC 1.1.1.44; 6-PGDH) from sheep liver is described. The enzyme is directly bound to cellulose phosphate by batch extraction and eluted with a linear salt gradient. Purification is completed by affinity chromatography using NADP(+)-agarose. The result is 6-PGDH of high purity, greatly increased yield, and the highest specific activity yet achieved, with a significant reduction in the purification time.