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1969•Biochemical JournalOpen access

Purification and properties of 6-phosphogluconate dehydrogenase from sheep liver

Ruxton H. Villet, Keith Dalziel

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Abstract

A method is described for the isolation of 6-phosphogluconate dehydrogenase from sheep liver. The product appears to be homogeneous in polyacrylamide-gel electrophoresis and in sedimentation-velocity and sedimentation-equilibrium studies in the ultracentrifuge. The molecular weight is estimated as 129000 from equilibrium sedimentation.

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A method is described for the isolation of 6-phosphogluconate dehydrogenase from sheep liver. The product appears to be homogeneous in polyacrylamide-gel electrophoresis and in sedimentation-velocity and sedimentation-equilibrium studies in the ultracentrifuge. The molecular weight is estimated as 129000 from equilibrium sedimentation.

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Available abstract

A method is described for the isolation of 6-phosphogluconate dehydrogenase from sheep liver. The product appears to be homogeneous in polyacrylamide-gel electrophoresis and in sedimentation-velocity and sedimentation-equilibrium studies in the ultracentrifuge. The molecular weight is estimated as 129000 from equilibrium sedimentation.

Key concepts: Ultracentrifuge, Sedimentation equilibrium, Sedimentation, Sedimentation coefficient, Homogeneous, Chromatography, Polyacrylamide gel electrophoresis, Biochemistry

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