May 1984
Volume 25, Issue 5
Articles  |   May 1984
Glutathione peroxidase of calf trabecular meshwork.
Investigative Ophthalmology & Visual Science May 1984, Vol.25, 599-602. doi:
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      D R Scott, L N Karageuzian, P J Anderson, D L Epstein; Glutathione peroxidase of calf trabecular meshwork.. Invest. Ophthalmol. Vis. Sci. 1984;25(5):599-602.

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      © ARVO (1962-2015); The Authors (2016-present)

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Glutathione peroxidase was extracted from calf trabecular meshwork. The kinetics of this enzyme were examined, varying the substrates hydrogen peroxide (H2O2), tert- butylhydroperoxide ( tBHP ), and glutathione. The activity of the enzyme in nonpurified homogenates was 596 nmole H2O2 reduced/min/gm wet weight and 680 nmole tBHP reduced/min/gm wet weight (27-28 nmole peroxide reduced/min/mg protein). The apparent Michaelis--Menten constants for H2O2, tBHP , and GSH were 0.012, 0.102, and 2.89 mM, respectively. These data, together with published levels of glutathione in trabecular meshwork, suggest that the trabecular endothelial cell actively detoxifies H2O2.


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