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Early research suggested that the tripeptide bonds of standard generic glutathione were rapidly degraded by peptidases and stomach acids in the gastrointestinal tract, leading to poor systemic bioavailability

Researchers rely on our formula to maintain the activity and stability of their compounds

The presence of the second active-site cysteinyl residue in PfGrx improves the reactivity of the ternary complex but does not form an intramolecular disulfide bond in contrast to a dithiol mechanism

It naturally occurs in most foods, including milk and dairy, salmon, poultry, eggs, spinach, and almonds

The "L" in L-glutathione refers to the molecular structure of the amino acids that build the compound