Glutathione Beads
Glutathione Beads - Related Videos
03:32
Amplified Luminescent Proximity Homogeneous Assay: A Bead-Based Proximity Assay to Screen Small Molecules Inhibiting Protein-Protein Interactions
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In this video, we demonstrate the amplified luminescent proximity homogeneous assay—a bead-based proximity assay. It utilizes homogeneously-sized acceptor and donor beads, immobilized with two proteins that tend to interact to screen potential small molecules inhibiting protein interactions.
08:10
Measuring Glutathione-induced Feeding Response in Hydra
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Cited by 9 •
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Here we describe a simple assay for the quantification of the feeding response in hydra induced by the reduced form of glutathione. This assay relies on measuring the distance between the apical end of the tentacle and mouth of hydra.
01:22
Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation
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2025
Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion. Several distinctive characteristics distinguish glutathione conjugation from other phase II...
14:57
Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
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Cited by 14 •
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Glutathione S-transferases (GSTs) are detoxification enzymes involved in the metabolism of numerous chemotherapeutic drugs. Overexpression of GSTs is correlated with cancer chemotherapy resistance. One way to counter this phenotype is to use inhibitors. This protocol describes a method using a spectrophotometric assay to screen for potential GST inhibitors.
11:52
Microbubble Fabrication of Concave-porosity PDMS Beads
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Cited by 2 •
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Procedures used to generate microstructured concave-porosity polydimethylsiloxane beads are presented. Effects of electrolyte concentration and identity within the aqueous phase are particularly emphasized.
FAQs
Selectivity comes from the interaction between the GST portion of a fusion protein and immobilized glutathione on the bead surface. Proteins lacking the relevant glutathione-binding property do not remain captured under the same conditions and can be removed during washing. This helps enrich the tagged recombinant protein from a complex cell lysate.
Washing separates captured GST fusion protein from molecules that remain in the lysate without the required binding interaction. The process depends on retaining the target on the immobilized glutathione while removing unbound components. Effective washing therefore improves sample purity before release, which is important for later biochemical studies of protein function or interactions.
Free glutathione provides an elution option after the target has been retained on the beads. Introducing it, or otherwise changing the binding conditions, causes the captured protein to be released from the bead-associated interaction. This separates the enriched GST fusion protein from the solid support and produces a fraction suitable for downstream biochemical analysis.
A typical workflow begins by passing a cell lysate containing the target fusion protein through the beads. The GST-tagged protein is retained, whereas unbound lysate components are removed during washing. The target is then recovered by adding free glutathione or changing the binding conditions, yielding an enriched protein preparation for further study.
The key sample is a cell lysate containing a recombinant protein with a GST tag. The essential processing stages are capture on immobilized glutathione, removal of unbound molecules by washing, and elution through free glutathione or altered binding conditions. Together, these steps use the tag-associated binding property to simplify purification from a complex mixture.
This approach is useful when researchers need to produce or enrich recombinant GST fusion proteins from cell lysates. The purified material can support studies of protein function and protein interactions, while the straightforward capture, wash, and release sequence also suits teaching laboratories. Its value comes from combining selective purification with a convenient experimental workflow.