[38] Oxidative damage to proteins: Spectrophotometric method for carbonyl assay

Reznick, Abraham Z.; Packer, Lester

doi:10.1016/s0076-6879(94)33041-7

Cited by 2,122 publications

(1,165 citation statements)

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“…Carbonyl protein content was measured as described by Reznick and Packer [25], with some modifications. Briefly, approximately 50 mg of cardiac muscle samples from control and tumour-bearing animals were placed in glass homogenization tubes containing 1 mL of homogenization buffer [50 mM phosphate buffer, 1 mM ethylenediaminetetraacetic acid, pH 7.4].…”

Section: Quantification Of Carbonyl Proteinmentioning

confidence: 99%

Oxidative and proteolytic profiles of the right and left heart in a model of cancer-induced cardiac cachexia

et al. 2014

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Section: Quantification Of Carbonyl Proteinmentioning

confidence: 99%

Oxidative and proteolytic profiles of the right and left heart in a model of cancer-induced cardiac cachexia

et al. 2014

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“…8). The results are usually expressed in moles of carbonyls per gram of proteins [82,83]. Such spectrophotometric assay is not exempt from biases, such as the presence of excess DNPH [84], or nonprotein carbonyls.…”

Section: Carbonyl Detection and Quantificationmentioning

confidence: 99%

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Barelli

Canellini

Thadikkaran

et al. 2008

Proteomics Clinical Apps

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Protein oxidation mechanisms result in a wide array of modifications, from backbone cleavage or protein crosslinking to more subtle modifications such as side chain oxidations. Protein oxidation occurs as part of normal regulatory processes, as a defence mechanism against oxidative stress, or as a deleterious processes when antioxidant defences are overcome. Because blood is continually exposed to reactive oxygen and nitrogen species, blood proteomics should inherently adopt redox proteomic strategies. In this review, we recall the biochemical basis of protein oxidation, review the proteomic methodologies applied to analyse redox modifications, and highlight some physiological and in vitro responses to oxidative stress of various blood components.

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“…Measurement of carbonyl formation was carried out by a modification of the method of Reznick & Packer (1994) which is based on the spectrophotometric detection of the reaction of dinitrophenylhydrazine (DNPH) with protein carbonyl to form protein hydrazones. Liver was prepared for analysis according to the method described recently (Cao & Cutler, 1995).…”

Section: Sample Collection and Analysismentioning

confidence: 99%

Cobalt–deficiency–induced hyperhomocysteinaemia and oxidative status of cattle

et al. 2000

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In ruminants, Co is required for the synthesis of vitamin B 12 , which in turn is needed for the resynthesis of methionine by methylation of homocysteine and thus, cobalamin deficiency may induce hyperhomocysteinaemia which is brought into context with perturbations of the antioxidative-prooxidative balance. The present study was conducted to explore whether Co deficiency in cattle is also associated with homocysteine-induced disturbances of oxidative status. Co deficiency was induced in cattle by feeding two groups of animals on either a basal maize-silage-based diet that was moderately low in Co (83 g Co/kg DM), or the same diet supplemented with Co to a total of 200 g Co/kg DM, for 43 weeks. Co deficiency was apparent from a reduced vitamin B 12 status in serum and liver and an accumulation of homocysteine in plasma which was in excess of 4⋅8 times higher in Co-deprived cattle than in controls. The much increased level of circulating homocysteine did not indicate severe disturbances in antioxidantprooxidant balance as measured by individual markers of lipid peroxidation, protein oxidation, and the antioxidative defence system. There were no quantitative difference in plasma thiol groups, nor were there significant changes in concentrations of a-tocopherol, microsomal thiobarbituric acid-reactive substances and carbonyl groups in liver. However, there was a trend toward increased plasma carbonyl levels indicating a slight degradation of plasma proteins in the hyperhomocysteinaemic cattle. Analysis of the hepatic catalase (EC 1.11.1.6) activity revealed an 11 % reduction in Co-deficient cattle relative to the controls. These results indicate that long-term moderate Co deficiency may induce a severe accumulation of plasma homocysteine in cattle, but considerable abnormalities in oxidative status failed to appear.

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[38] Oxidative damage to proteins: Spectrophotometric method for carbonyl assay

Cited by 2,122 publications

References 10 publications

Oxidative and proteolytic profiles of the right and left heart in a model of cancer-induced cardiac cachexia

Oxidative and proteolytic profiles of the right and left heart in a model of cancer-induced cardiac cachexia

Oxidation of proteins: Basic principles and perspectives for blood proteomics

Cobalt–deficiency–induced hyperhomocysteinaemia and oxidative status of cattle

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