Microsomal glutathione S-transferase is the predominant leukotriene C4 binding site in cellular membranes.

Identification of a high affinity leukotriene C4-binding protein in rat liver cytosol as glutathione S-transferase.

A soluble high affinity binding unit for leukotriene (LT) C4 in the high speed supernatant of rat liver homogenate was characterized at 4 degrees C as having a single type of saturable affinity site with a dissociation constant of 0.77 +/- 0.27 nM (mean +/- S.E., n = 5). The binding activity was identified as the liver cytosolic subunit 1 (Ya) of glutathione S-transferase, commonly known as lig...

Binding of glutathione and an inhibitor to microsomal glutathione transferase.

Microsomal glutathione transferase is an abundant liver protein that can be activated by thiol reagents. It is not known whether the activation is associated with changed binding properties of the enzyme. Therefore the binding of GSH and an inhibitor to rat liver microsomal glutathione transferase was studied by use of equilibrium dialysis and equilibrium partition in a two-phase system. The ra...

Cellular Immune Responses in Sheep against Glutathione S-transferase of Fasciola gigantica

Immunolocalization of microsomal glutathione S-transferase in rat tissues.

Distribution of microsomal glutathione transferase (mGST) protein in rat tissues was investigated by immunohistochemistry. Studies on the localization of mGST are of interest because of its involvement in the detoxication and bioactivation of xenobiotics. mGST antigen was detected in the cytoplasm of some hepatocytes and in bile ducts. In kidney, focal staining of mGST was observed in distal tu...

Inhibition and recognition studies on the glutathione-binding site of equine liver glutathione S-transferase.

Equine liver glutathione S-transferase has been shown to consist of two identical subunits of apparent Mr 25,500 and a pl of 8.9. Kinetic data at pH 6.5 with 1-chloro-2,4-dinitrobenzene as a substrate suggests a random rapid-equilibrium mechanism, which is supported by inhibition studies using glutathione analogues. S-(p-Bromobenzyl)glutathione and the corresponding N alpha-, CGlu- and CGly-sub...