Glutathione S-Transferase from human placenta

Glutathione S-transferase (GST) is a major detoxification enzyme, and exists as multiple cytoplasmic and membrane-bound isozymes. Cytoplasmic isoforms of GST are encoded by five genes, namely α, γ, μ, σ and π. α, μ and π are the most abundant forms in mammals. GSTπ is the isoform of this enzyme found in placenta and is composed of 209 amino acids.

Glutathione S-transferase mu 1 (GSTM1) is mapped to human chromosome 1p13.3.

Glutathione S-Transferase from human placenta has been used for the immunization of rabbits for the production of specific anti-π-GST antibodies, to determine whether total anti-π-GST antibodies are more specific and reactive as compared to anti-peptide antibodies.

Glutathione S-Transferase from human placenta has been used in antigen microarray and informatics analysis.

Glutathione S-transferase (GST) catalyzes conjugation reactions during phase II metabolism. This enzyme also confers protection against catabolic products of peroxidized lipid and oxidized DNA, and ROS (reactive oxygen species) or electrophiles.

Glutathione S-transferase (GST) catalyzes the reduction of dehydroascorbic acid to ascorbic acid in the presence of glutathione. GST exhibits neuroprotective action, by eliminating oxidants (exogenous and endogenous), detoxifying therapeutic drugs and other toxins in the environment. Mutation in this gene is known to cause epilepsy. Deletion of the gene may result in cancer.

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

Glutathione S-transferases are a protein family catalyzing conjugation of reduced glutathione with various hydrophobic chemicals.

Lyophilized powder containing Tris buffer salts, reduced glutathione and EDTA.

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.

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.