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Updated: Aug 19, 2026

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Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
The purification of yeast glucose 6-phosphate dehydrogenase by dye-ligand chromatography
Analytical Biochemistry
|August 15, 1984
Abstract:
Glucose 6-phosphate dehydrogenase (EC 1.1.1.39) has been purified to homogeneity from baker's yeast by a simple procedure involving affinity elution from a column of red triazine dye, H-8BN, immobilized to Sepharose 6B. Eight milligrams of homogeneous protein is obtained in 53% yield from 200 g of dried yeast. This represents the first published purification of the enzyme from Saccharomyces Cerevisiae.

