L-Glutathione

L-Glutathione Overview

L-Glutathione is a ubiquitous tripeptide present in virtually all living organisms, serving as a primary intracellular antioxidant and redox regulator. In its reduced form (GSH), it participates in neutralizing reactive oxygen species (ROS), maintaining redox homeostasis, and supporting the integrity of proteins, lipids, and DNA against oxidative stress. Through its sulfhydryl group on the cysteine residue, glutathione acts as a substrate for peroxidase enzymes that reduce hydrogen peroxide and lipid peroxides. Research models examine its role in phase II conjugation pathways, molecular proliferation and signaling, mitochondrial function, and protein folding regulation in laboratory settings. Forman et al. (2009).

Lu (2013).

History

Glutathione was first discovered in 1888 by J. de Rey-Pailhade as a sulfur-containing compound in yeast and animal tissues, initially termed "philothion." The complete chemical structure as a γ-glutamylcysteinylglycine tripeptide was elucidated in 1935 by Frederick Gowland Hopkins, who received the Nobel Prize for his contributions to vitamin discovery. Since then, glutathione has been recognized as a fundamental molecule in cellular biochemistry and redox biology.

Meister & Anderson (1983).

L-Glutathione Structure

CAS #:

70-18-8

Molecular Formula:

C₁₀H₁₇N₃O₆S

Molecular Weight:

307.32 g/mol

PubChem ID:

124886