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Merck

G6511

Glutathione S-Transferase from equine liver

lyophilized powder, ≥25 units/mg protein

Synonyme(s) :

GST, Glutathione R-transferase, Glutathione S-alkenetransferase, Glutathione S-alkyltransferase, Glutathione S-aralkyltransferase, Glutathione S-aryltransferase, Glutathione S-epoxidetransferase

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.47
Numéro CE :
MDL number:
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biological source

equine liver

Quality Segment

form

lyophilized powder

specific activity

≥25 units/mg protein

mol wt

45-50 kDa

composition

Protein, ≥60%

storage temp.

−20°C

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.

Biochem/physiol Actions

Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers.
Protein family catalyzing conjugation of reduced glutathione with various hydrophobic chemicals.
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 atracurium
  • as a component of GSB stock solution to determine GSB (glutathione S-bimane) conjugate fluorescence intensity in intact Arabidopsis cells
  • as an enzyme standard in spectrophotometric assay to determine the activity of GST

Physical form

Lyophilized powder containing Tris, reduced glutathione and EDTA.

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.

Other Notes

One unit will conjugate 1.0 μmole of 1-chloro-2,4-dinitrobenzene with reduced glutathione per min at pH 6.5 at 25°C.


pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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