| Name | hemoglobin (protein family or complex) |
|---|---|
| Synonyms | Hemoglobin; Hemoglobins |
| Name | amitrole |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 7682576 | Scott MD, van den Berg JJ, Repka T, Rouyer-Fessard P, Hebbel RP, Beuzard Y, Lubin BH: Effect of excess alpha-hemoglobin chains on cellular and membrane oxidation in model beta-thalassemic erythrocytes. J Clin Invest. 1993 Apr;91(4):1706-12. |
8(0,0,0,8) | Details |
| 16274876 | Johnson RM, Goyette G Jr, Ravindranath Y, Ho YS: Hemoglobin autoxidation and regulation of endogenous H2O2 levels in erythrocytes. Free Radic Biol Med. 2005 Dec 1;39(11):1407-17. Epub 2005 Aug 24. |
3(0,0,0,3) | Details |
| 2840755 | Runge-Morris MA, Iacob S, Novak RF: Characterization of hydrazine-stimulated proteolysis in human erythrocytes. Toxicol Appl Pharmacol. 1988 Jul;94(3):414-26. These data suggest that more reactive free radicals generated from the hydrazine are responsible for protein damage, that damaged protein (hemoglobin) is degraded via proteolysis, and that an ATP-independent process primarily participates in the degradation of abnormal proteins in the red cell. |
2(0,0,0,2) | Details |
| 489671 | Mager D, Bernstein A: The role of heme in the regulation of the late program of Friend cell erythroid differentiation. J Cell Physiol. 1979 Sep;100(3):467-79. The addition of a chemical inducer, such as dimethylsulfoxide (DMSO), to cultures of mouse Friend erythroleukemic cells results in the induction of a number of late erythroid events, including the accumulation of globin mRNA, the inducation of hemoglobin synthesis, the appearance of erythrocyte membrane antigens (EMA), and the cessation of cell division. |
2(0,0,0,2) | Details |
| 49150 | Breton-Gorius J, Guichard J: Fine structural and cytochemical identification of microperoxisomes in developing human erythrocytic cells. Am J Pathol. 1975 Jun;79(3):523-36. Optimal conditions for the visualization of these granules by incubation in alkaline DAB were obtained when the peroxidase activity of hemoglobin was reduced by addition of low concentrations of |
2(0,0,0,2) | Details |
| 2764932 | Orii Y, Sakai Y, Ozawa K: Ubiquitous formation of catalase compound II in hemoglobin-free perfused rat liver and detection of novel spectral species. Biochem Biophys Res Commun. 1989 Aug 15;162(3):1272-8. |
2(0,0,0,2) | Details |
| 16545695 | Scott MD: H2O2 injury in beta thalassemic erythrocytes: protective role of catalase and the prooxidant effects of GSH. Free Radic Biol Med. 2006 Apr 1;40(7):1264-72. Epub 2005 Dec 19. Because of the autoxidation of the unstable hemoglobin chains and subsequent release of globin free heme and iron, significant amounts of (O2-) and, more importantly, peroxide (H2O2) are generated intracellularly. |
2(0,0,0,2) | Details |
| 8896899 | Masuoka N, Wakimoto M, Ubuka T, Nakano T: Spectrophotometric determination of peroxide: catalase activity and rates of peroxide removal by erythrocytes. Clin Chim Acta. 1996 Oct 29;254(2):101-12. From the measurement of catalase activity in erythrocytes treated with 3-amino-1,2,4-triazole and rates of peroxide removal by the erythrocytes, it is deduced that rate constants related to the hemoglobin content (k/g Hb) for peroxide removal by catalase in normal and acatalasemic erythrocytes are 42.0 +/- 6.0 and 8.0 +/- 3.0, respectively. |
1(0,0,0,1) | Details |
| 1417978 | Marcocci L, Pietrangeli P, Mavelli I, Rotilio G: Plasma membrane as a site of redox activation of daunomycin in intact human erythrocytes. Biochem Pharmacol. 1992 Oct 20;44(8):1535-42. The relative importance in human red blood cells of the plasma membrane as a site of redox activation of anthracyclines as compared to hemoglobin was evaluated by assaying the H2O2 produced upon exposure to daunomycin. |
1(0,0,0,1) | Details |
| 17123644 | Citelli M, Lara FA, da Silva Vaz I Jr, Oliveira PL: Oxidative stress impairs heme detoxification in the midgut of the cattle tick, Rhipicephalus (Boophilus) microplus. Mol Biochem Parasitol. 2007 Jan;151(1):81-8. Epub 2006 Nov 13. Hydrolysis of hemoglobin in the digestive vesicles of these cells results in the release of large amounts of heme, a pro-oxidant compound, whose iron atom, together with H (2) O (2), may participate in the Fenton reaction and lead to the production of |
1(0,0,0,1) | Details |