Related Experiment Video
Updated: Aug 9, 2026

Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
S-(1,2-Dicarboxyethyl)glutathione in yeast: partial purification of its synthesizing enzyme
Abstract:
S-(1,2-Dicarboxyethyl)glutathione (DCE-GS) was found in Saccharomyces cerevisiae, but not in bacterial species nor in a unicellular alga (Acetabularia acetabulum). The enzyme that catalyzes condensation of L-malate and glutathione (GSH) to form DCE-GS was partially purified from baker's yeast. It had a molecular mass of 49 kDa and was monomeric and the Km values were 2.2 and 1.4 mM for L-malate and GSH, respectively. The enzyme had a pH optimum of 7.5. DCE-GS levels in yeast cells were significantly higher in aerobic cultures than in anaerobic ones. DCE-GS was synthesized in cells cultured between 20 and 35 degrees C.
More Related Videos
09:22Budding Yeast Protein Extraction and Purification for the Study of Function, Interactions, and Post-translational Modifications
Published on: October 30, 2013
11:57Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase
Published on: June 24, 2025