BIOXYTECHÒ GR-340™
Kits
- 貨號 Cat. No.
- 21018
- 規格 Size
- 100 tests
- 品牌 Brand
- No Brand
Description
Glutathione reductase (GR, EC 1.6.4.2) is a ubiquitous enzyme, which catalyzes the reduction of
oxidized glutathione (GSSG) to glutathione (GSH). Glutathione reductase is essential for the
glutathione redox cycle that maintains adequate levels of reduced cellular GSH. GSH serves as
an antioxidant, reacting with free radicals and organic peroxides, in amino acid transport, and as
a substrate for the glutathione peroxidases and glutathione S-transferases in the detoxification of
organic peroxides and metabolism of xenobiotics, respectively.1
This homodimeric enzyme is a member of the family of flavoprotein disulfide oxidoreductases.
Each subunit has four domains; beginning at the N-terminus: an FAD-binding domain, an
NADPH-binding domain, a central domain, and an interface domain. The active site of GR is at
the dimeric interface. Since the GSSG binding site is composed of residues from both subunits,
only the dimeric form is active.2
oxidized glutathione (GSSG) to glutathione (GSH). Glutathione reductase is essential for the
glutathione redox cycle that maintains adequate levels of reduced cellular GSH. GSH serves as
an antioxidant, reacting with free radicals and organic peroxides, in amino acid transport, and as
a substrate for the glutathione peroxidases and glutathione S-transferases in the detoxification of
organic peroxides and metabolism of xenobiotics, respectively.1
This homodimeric enzyme is a member of the family of flavoprotein disulfide oxidoreductases.
Each subunit has four domains; beginning at the N-terminus: an FAD-binding domain, an
NADPH-binding domain, a central domain, and an interface domain. The active site of GR is at
the dimeric interface. Since the GSSG binding site is composed of residues from both subunits,
only the dimeric form is active.2
