Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Földes-Papp, Z; Maretzki, D.
Enzymatic t-butyl hydroperoxide reduction on human erythrocyte membranes--NADPH and GSH dependent activities.
Biomed Biochim Acta. 1984; 43(3): 271-279.
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- Földes-Papp Zeno
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- 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.
- Find related publications in this database (using NLM MeSH Indexing)
- Catalase - blood
- Erythrocyte Membrane - metabolism
- Glutathione - blood
- Glutathione Peroxidase - blood
- Hemoglobins - metabolism
- Humans - metabolism
- NADP - blood
- Oxidation-Reduction - blood
- Peroxides - blood
- tert-Butylhydroperoxide - blood