Stimulatory effect of histone on glutathione reductase of human erythrocytes.
Glutathione reductase of hemolyzates, as well as intact erythrocytes from normal individuals can be activated by the addition of human leukocyte nuclear histones and histone subfractions f1 and f3. Intact erythrocytes incubated with histone show also in their hemolyzates a high glutathione reductase activity as compared with such not treated with histone cells. The degree of stimulation of glutathione reductase by histones is comparable to that caused by flavin adenosine diphosphate (FAD). Histones  and FAD show a competitive stimulatory effect on glutathione reductase activity. ATP shows an inhibitory effect on glutathione reductase activity, which can be reversed by addition of histone.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004912:Erythrocytes / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide / Q000494:pharmacology; D005980:Glutathione Reductase / Q000097:blood*; D006657:Histones / Q000494:pharmacology*; D006801:Humans; D066298:In Vitro Techniques; D007962:Leukocytes / Q000648:ultrastructure; D013268:Stimulation, Chemical
D006657:Histones; D005182:Flavin-Adenine Dinucleotide; D000255:Adenosine Triphosphate; D005980:Glutathione Reductase