Not available outside of the UK & Ireland.

Analysis Note

Protein determined by biuret.Purified and assayed by a modification of the method of Simons and Vander Jagt.Enzymatic activities are based on the conjugation of reduced glutathione with a second substrate. The individual proteins generally have activity with more than one class of substrate.

Biochem/physiol Actions

Glutathione S-transferase (GST) from equine liver has been used-as a constituent of Tris buffer for incubation of human umbilical vein endothelial cells (HUVEC) with atracurium to assess the proliferation of HUVEC in the presence of atracuriumas a component of GSB stock solution to determine GSB (glutathione S-bimane) conjugate fluorescence intensity in intact Arabidopsis cellsas an enzyme standard in spectrophotometric assay to determine the activity of GST

Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers.

General description

Glutathione S-transferase (GST) is a major detoxification enzyme, and exists as multiple cytoplasmic and membrane-bound isozymes. These isozymes differ in their catalytic activity, as well as in their non-catalytic binding properties. Cytoplasmic isoforms of GST are encoded by five genes, namely α, θ, μ, σ and π. α, μ and π are the most abundant forms in mammals. Membrane bound GST forms are encoded by a single gene.

Packaging

1, 5, 10 mg in glass bottle

25 mg in poly bottle

Physical form

Lyophilized powder containing Tris, reduced glutathione and EDTA.

Unit Definition

One unit will conjugate 1.0μmole of 1-chloro-2,4-dinitrobenzene with reduced glutathione per min at pH6.5 at 25°C.