Glutathione and How it Protects Mammalian Organisms from Potentially Toxic Compounds (Research Paper Sample)

Discuss The Different Ways Glutathione Acts to Protect Mammalian Organisms from Potentially Toxic Compounds
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November 3, 2022
Discuss the Different Ways Glutathione Acts to Protect Mammalian Organisms from Potentially Toxic Compounds
The most prevalent non-protein thiol in mammalian cells is glutathione having a concentration of around 5 mmol per gram of tissue. The concentration of glutathione is comparable to the quantity of glucose in cells. A tripeptide that dissolves in water is the reduced form of glutathione (GSH). Since there are fewer gamma-peptidases than alpha-peptidases in living organisms, glutathione is stabilized by the gamma link between glutamic acid and cysteine. The most significant thiol, glutathione, functions as a reactant, reducing agent, and catalyst. The liver, kidney, lungs, and intestines are just a few of the organs that contain a significant amount of this molecule. However, glutathione quantities in bodily fluids are at micromolar levels (Erkekoglu, 2018).
Glutathione Structure
Glutathione serves as an antioxidant, free radical scavenger, and detoxifying agent. It also functions as a cofactor for the glutathione peroxidase enzyme that forms leukotrienes, and is essential for amino acid absorption. The tripeptide glutathione, which is composed of the three amino acids cysteine, glutamic acid, and glycine, is found in the majority of mammalian organs. The structure of glutathione is shown in figure 1. The carboxyl group of glutamate links the N-terminal glutamate and cysteine in the reduced form, blocking breakdown by common cellular peptidases and limiting cleavage to glutamyltranspeptidase. A reactive thiol group that is crucial to glutathione's actions is provided by cysteine, which is its primary functional element. Furthermore, the intermolecular dipeptide link in the oxidized glutathione molecule is formed by cysteine residues (Lushchak, 2012).
Figure 1
Structure of Glutathione
Structure of Glutathione (Lushchak, 2012)
Glutathione Biosynthesis
A metabolic process for GSH's synthesis from its three amino acids is depicted in Figure 2. The rate-limiting step in Glutathione biosynthesis is the presence of cysteine and its constituent methionine, according to a research study utilizing radioisotopes. Generally speaking, it is believed that the levels of gamma-glutamyl-cysteine synthetase and the amino acid