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Oxidized Proteins in Alzheimer's Plasma

Biochemical and Biophysical Research Communications, 2000
The levels of oxidatively modified proteins were examined in blood from Alzheimer's disease (AD) patients, non-AD controls, and AD relatives. Oxidative modification was measured by reacting the protein carbonyls with 2,4-dinitrophenyl hydrazine (DNPH).
C C, Conrad   +5 more
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Immunochemical detection of oxidized proteins

Chemical Research in Toxicology, 1993
An immunochemical assay was developed to detect carbonyl moieties that result from oxidative damage to proteins. Bovine serum albumin was reacted with hydroxyl radicals generated via a Fenton-like mechanism or by a radiolysis mechanism. The resulting albumin-derived carbonyls were reacted with 2,4-dinitrophenylhydrazine, giving the corresponding ...
R J, Keller   +3 more
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Oxidative haemolysis in protein malnutrition

Clinica Chimica Acta, 1981
A study of the haemolytic anaemia observed in protein-energy malnutrition (PEM) in Kivu disclosed the following results. The in vitro resistance to oxidative aggressions of PEM patients' erythrocytes was decreased: when incubated with acetylphenylhydrazine, a higher percentage of the cells showed Heinz bodies, as compared with erythrocytes of local ...
Vertongen, Françoise   +3 more
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Performic Acid Oxidation of Proteins

Cold Spring Harbor Protocols, 2007
INTRODUCTIONDisulfide bond cleavage is a prerequisite to many peptide-mapping strategies. It facilitates protein unfolding and thus optimizes proteolytic digestion. It also simplifies the interpretation of peptide maps by removing possible peptide fragment(s) in the mixture that are held together by disulfide bonds.
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Oxidized protein aggregates

2020
The study of protein aggregates has a long history. While in the first decades until the 80ies of the 20th century only the observation of the presence of such aggregates was reported, later the biochemistry of the formation and the biological effects of theses aggregates were described.
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Oxidative modifications of protein structures

2001
Publisher Summary This chapter discusses the oxidative modifications and biological effects of protein structures. Proteins undergo oxidative modifications due to the complexity of their chemical structures in subsequent stages which depend on the presence of oxidation, susceptible groups and on steric availability of these groups for oxidant attacks.
J W, Naskalski, G, Bartosz
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Protein glutathionylation and oxidative stress

Journal of Chromatography B, 2007
Liquid chromatography/electrospray ionization-mass spectrometry (LC/ESI-MS) demonstrated that glutathionyl hemoglobin (Hb) levels are increased in patients with diabetes, hyperlipidemia, uremia and Friedreich's ataxia. Glutathionylation of Hb is enhanced by oxidative stress.
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Oxidative protein folding

2019
Disulfide bond formation on luminal proteins in thylakoids 1240 V. Conclusion 1242 Acknowledgements 1242 References 1242 SUMMARY: Disulfide bonds are post-translational modifications crucial for the structure and function of thousands of proteins. Their formation and isomerization, referred to as oxidative folding, require specific protein machineries ...
Meyer, Andreas J   +2 more
openaire   +1 more source

Protein Oxidation Products as Biomarkers

Free Radical Biology and Medicine, 2014
Oxidative stress is associated with aging and most degenerative diseases: it contributes to clinical complications, organ failure and mortality. Furthermore, oxidative damage accumulation in macromolecules has been considered as a cause of cellular damage and pathology.
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Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation

Comprehensive Reviews in Food Science and Food Safety, 2021
Yulong Bao   +2 more
exaly  

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