• Publications
  • Influence
Determination of carbonyl content in oxidatively modified proteins.
TLDR
This chapter discusses methods to determine carbonyl content in oxidatively modified proteins and quantitated protein-bound pyruvoyl groups through formation of a Schiff base with p-aminobenzoic acid followed by reduction with cyanoborohydride. Expand
Carbonyl assays for determination of oxidatively modified proteins.
TLDR
New methods for determination ofcarbonyl content are presented, which are based on the reaction of carbonyl groups with 2,4-dinitrophenylhydrazine to form a 2, 4-d Initrophenolhydrazone, which provide substantial improvements in both sensitivity and specificity. Expand
Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
TLDR
It is evident that the cyclic oxidation and reduction of the sulfur-containing amino acids may serve as an important antioxidant mechanism, and also that these reversible oxidations may provide an important mechanism for the regulation of some enzyme functions. Expand
Methionine residues as endogenous antioxidants in proteins.
TLDR
This work proposes that methionine residues constitute an important antioxidant defense mechanism, and investigates the effect of hydrogen peroxide exposure upon glutamine synthetase from Escherichia coli as an in vitro model system. Expand
Small-Molecule Antioxidant Proteome-Shields in Deinococcus radiodurans
TLDR
By establishing that Mn2+-metabolite complexes of D. radiodurans specifically protect proteins against indirect damage caused by gamma-rays delivered in vast doses, the findings provide the basis for a new approach to radioprotection and insight into how surplus Mn budgets in cells combat reactive oxygen species. Expand
Carbonyl modified proteins in cellular regulation, aging, and disease.
  • R. L. Levine
  • Chemistry, Medicine
  • Free radical biology & medicine
  • 1 May 2002
TLDR
The oxidative modification of proteins by reactive species is implicated in the etiology or progression of a panoply of disorders and diseases and can be quantitated by measurement of the protein carbonyl content, which has been shown to increase in a variety of diseases and processes, notably during aging. Expand
Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence.
TLDR
Analysis of the fluorescence characteristics of ethidium (E(+)) and 2-OH-E(+) strongly suggests that the currently available fluorescence methodology is not suitable for quantitating intracellular O(2)(.-). Expand
Protein Oxidation
TLDR
The oxidative modification of proteins by reactive species, especially reactive oxygen species, is implicated in the etiology or progression of a panoply of disorders and diseases, most notably during aging. Expand
Oxidative damage during aging targets mitochondrial aconitase.
TLDR
It is shown that mitochondrial aconitase, an enzyme in the citric acid cycle, is a specific target of oxidative damage during aging of the housefly and allows for the assessment of the physiological age of a specific individual and provides a method for the evaluation of treatments designed to affect the aging process. Expand
Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins.
TLDR
Results indicate that glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins, and that this reaction is a major route leading to the generation of protein carbonyls in biological samples. Expand
...
1
2
3
4
5
...