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Glutathione is the primary component of glutathione peroxidase, one of the most powerful antioxidant enzymes in our bodies

This knowledge coupled with the demonstration that some members of the 6-AH family bound with high affi nity to the hinge region of HGF led to the expectation that other active AnglV analogs, like 6-AH family members, could be expected to inhibit HGF dimerization and that the ability of an individual analog to bind HGF and inhibit HGF-dependent processes should be reflected in its capacity to attenuate dimerization

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