Improved direct specific determination of serum iron and total iron-binding capacity.

Ceriotti, Ferruccio; Ceriotti, G

doi:10.1093/clinchem/26.2.327

Cited by 62 publications

(25 citation statements)

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“…In this regard, the amount of thiobarbituric acid reactive (TBAR) products increased by 3.5-and 5-fold respectively for EGM of normal and NIDDM individuals. Non-heme iron was estimated by a modification of the ferrozine assay described by Ceriotti and Ceriotti (1980) and expressed as nmoles non-heme iron per mg protein. Mean and standard deviation of 15 preparations are given.…”

Section: Resultsmentioning

confidence: 99%

“…Membrane-bound non-heme iron was determined according to a modified method of Ceriotti and Ceriotti (1980) [14]. Final concentration of reagents used were 38 mM ascorbate, 0.67% sodium dodecyl sulphate, 10 mM phosphate buffer pH 7.4, 150 mM NaCl and 1.28 mM ferrozine (3-(2-pyridyl)-5,6-bis-(4-phenylsulfonic acid) 1,2,4-triazine) in a total volume of 3 ml.…”

Section: Determination Of Erythrocyte Ghost Membrane-bound Non-heme Ironmentioning

confidence: 99%

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Iron-Induced Oxidative Stress in Erythrocyte Membranes of Non-Insulin-Dependent Diabetic Nigerians

1999

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The presence of higher level of endogenous free radical reaction products in the erythrocyte ghost membrane (EGM) of Non-insulin-dependent diabetes mellitus (NIDDM) subjects compared with that of normal healthy controls has been demonstrated. The EGMs of NIDDM subjects were also shown to be more susceptible to exogenously generated oxidative stress than those of normal healthy individuals. The decreased level of reactive thiol groups in the EGM of NIDDM individuals supported this observation. We propose that the presence of significant levels of non-heme iron in the EGM of NIDDM subjects is an indication of the potential for iron-catalysed production of hydroxy and other toxic radicals which could cause continuous oxidative stress and tissue damage. Oxygen free radicals could therefore be responsible for most of the erythrocyte abnormalities associated with non-insulin-dependent diabetes and could indeed be intimately involved in the mechanism of tissue damage in diabetic complications.

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Section: Resultsmentioning

confidence: 99%

Section: Determination Of Erythrocyte Ghost Membrane-bound Non-heme Ironmentioning

confidence: 99%

Iron-Induced Oxidative Stress in Erythrocyte Membranes of Non-Insulin-Dependent Diabetic Nigerians

1999

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“…Visible spectra were recorded on a Beckman DU-70 recording spectrophotometer. Haem destruction was assessed as the amount of non-haem iron released into the reaction medium by use of the ferrozine assay (Ceriotti & Ceriotti, 1980). The reaction between H202 and the thiol compounds was investigated by determining the amount of unreacted thiol remaining at a given time point using the thiol assay of Haest et al (1978).…”

Section: Methodsmentioning

confidence: 99%

The formation of free radicals by cardiac myocytes under oxidative stress and the effects of electron-donating drugs

Turner

Rice‐Evans

Davies

et al. 1991

Biochemical Journal

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The interaction of myoglobin with H2O2 leads via a two-electron oxidation process to the formation of ferryl myoglobin. Metmyoglobin is more readily activated than oxymyoglobin to the ferryl states, which are capable of inducing peroxidative damage to membranes. E.p.r. and optical spectroscopic studies show that the thiol-containing compounds N-(2-mercaptopropionyl) glycine and N-acetylcysteine and the trihydroxamate desferrioxamine attenuate these processes by reducing the ferryl myoglobin species to metmyoglobin, with the formation of thiyl radicals and the desferrioxamine nitroxide radical respectively. Biochemical investigations of the potential for myoglobin in ruptured myocytes to be involved in radical generation, when under oxidative stress, and of the nature of the resulting species, were also undertaken. E.p.r. spectroscopic studies revealed the formation of a radical species which is capable of inducing membrane lipid peroxidation. The interaction of the thiol compounds and desferrioxamine with components of myocardial tissue under these conditions results in the generation of thiol-derived radical species and the desferrioxamine nitroxide radical respectively. These data, along with those obtained using optical spectrocopy, support the assignment of the identity of the radical species generated from the myocytes as the ferryl myoglobin radical.

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“…Membrane-associated non-haem iron was assayed utilising a modification of the ferrozine assay [21] at pH 7.4 in 10 mM phosphate-buffered saline with sodium dodecyl sulphate (0.67% w/v) to solubilise membranes. The absorbance at 562 nm was monitored as a function of time.…”

Section: Methodsmentioning

confidence: 99%

Desferrioxamine as a lipid chain‐breaking antioxidant in sickle erythrocyte membranes

1990

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The mechanism of action of desferrioxamine in the inhibition of the catalysis of iron-induced oxidative damage has been ascribed to its ability to chelate available ferric ion (&= 1Cri). However, recent work has proposed that the trihydroxamate moiety of desferrioxamine can also be involved in electron transfer reactions involving the superoxide radical, peroxidase/hydrogen peroxide mixtures and ferry1 myoglobin radicals. In this study we report evidence for the ability of desferrioxamine to inhibit peroxidative damage to pathological membranes with which non-haem iron is associated through a mechanism of action as a lipid chain breaking antioxidant, independently of its iron chelating properties.

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Improved direct specific determination of serum iron and total iron-binding capacity.

Cited by 62 publications

References 0 publications

Iron-Induced Oxidative Stress in Erythrocyte Membranes of Non-Insulin-Dependent Diabetic Nigerians

Iron-Induced Oxidative Stress in Erythrocyte Membranes of Non-Insulin-Dependent Diabetic Nigerians

The formation of free radicals by cardiac myocytes under oxidative stress and the effects of electron-donating drugs

Desferrioxamine as a lipid chain‐breaking antioxidant in sickle erythrocyte membranes

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