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- W2435752608 abstract "A NADPH-dependent t-butyl hydroperoxide ( TBH )-reducing activity independent of glutathione was found in addition to glutathione peroxidase activity bound to erythrocyte membranes. In hypotonic and isotonic membranes the NADPH-dependent TBH -reducing activity amounted to about 0.34 mu kat /l red blood cells (RBC) and the glutathione peroxidase activity to 0.32 mu kat /l RBC. The activities do not appear to be additive. The membrane association of the enzymes is independent of ionic strength. Under hypotonic condition about 0.2% of the total cellular catalase activity were bound to the membrane but none in isotonic membranes. The bound catalase appears to exhibit a glutathione dependent peroxidase activity. Membrane-bound haemoglobin exhibited a quasi- TBH -reductase activity which was inhibited by azide and cyanide." @default.
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- W2435752608 date "1984-01-01" @default.
- W2435752608 modified "2023-09-23" @default.
- W2435752608 title "Enzymatic t-butyl hydroperoxide reduction on human erythrocyte membranes--NADPH and GSH dependent activities." @default.
- W2435752608 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6743303" @default.
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