Glutathione peroxidase of calf trabecular meshwork.


Journal Article

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.

Full Text

Cited Authors

  • Scott, DR; Karageuzian, LN; Anderson, PJ; Epstein, DL

Published Date

  • May 1, 1984

Published In

Volume / Issue

  • 25 / 5

Start / End Page

  • 599 - 602

PubMed ID

  • 6715135

Pubmed Central ID

  • 6715135

Electronic International Standard Serial Number (EISSN)

  • 1552-5783

International Standard Serial Number (ISSN)

  • 0146-0404


  • eng