Tryptophan and Cysteine residues mediate chain reactions and propagation of oxidative damage in concentrated casein solutions

2021 ◽  
Vol 177 ◽  
pp. S62
Author(s):  
Eduardo Fuentes-Lemus ◽  
Shuwen Jiang ◽  
Per Hägglund ◽  
Michael J. Davies
Keyword(s):  
Oxidative Damage ◽  
Cysteine Residues ◽  
Chain Reactions

scholarly journals NADH:ubiquinone oxidoreductase from bovine mitochondria. cDNA sequence of a 19 kDa cysteine-rich subunit

1991 ◽  
Vol 277 (1) ◽  
pp. 11-15 ◽  
Author(s):  
A Dupuis ◽  
J M Skehel ◽  
J E Walker
Keyword(s):  
Complex I ◽  
Cysteine Residues ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Mature Protein ◽  
Chain Reactions ◽  
Polymerase Chain Reactions ◽  
Bovine Heart ◽  
Methionine Residue ◽  
New Strategy ◽  
Polymerase Chain

The sequence of a 19 kDa subunit of NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria has been determined by a new strategy based on the polymerase chain reaction. The subunits of the enzyme were resolved in a polyacrylamide gel by two-dimensional isoelectric focusing and electrophoresis under denaturing conditions, transferred to a poly(vinylidene difluoride) membrane, and the N-terminal sequence was determined on the stained 19 kDa protein up to residue 27. This information was used to design two mixed oligonucleotide primers and a mixed oligonucleotide probe. With total bovine heart cDNA as template, overlapping cDNAs extending to sequences corresponding to both the 5′ and 3′ extremities of the mRNA coding for the 19 kDa subunit were synthesized in three polymerase chain reactions. These cDNAs were cloned and sequenced and encode a 171-amino-acid mature protein preceded by a methionine residue. The mature protein contains eight cysteine residues spaced at regular intervals through the protein, but the cysteine-rich motifs that are often associated with tetranuclear or binuclear centres in other proteins are not present. However, all eight cysteine residues are strictly conserved in a related protein from Neurospora crassa, suggesting that they have structural and/or functional significance in complex I.

Oxygen toxicity: a radical explanation.

1998 ◽  
Vol 201 (8) ◽  
pp. 1203-1209 ◽  
Author(s):  
I Fridovich
Keyword(s):  
Free Radical ◽  
Oxidative Damage ◽  
De Novo ◽  
Oxygen Toxicity ◽  
Reactive Intermediates ◽  
Superoxide Dismutases ◽  
Radical Chain ◽  
Chain Reactions ◽  
De Novo Biosynthesis ◽  
Defensive Enzymes

During its reduction to water, O2 readily gives rise to dangerously reactive intermediates. This threat is diminished by families of defensive enzymes which include the superoxide dismutases, catalases and peroxidases. Free radical chain reactions are controlled by antioxidants, such as ascorbate and the tocopherols, and oxidative damage, which occurs in spite of these defenses, is largely repaired or is nullified by de novo biosynthesis. Yet some damage is sustained and it contributes to mutagenesis, to senescence and to numerous pathological processes.

scholarly journals Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage

FEBS Journal ◽  
2010 ◽  
Vol 277 (6) ◽  
pp. 1465-1480 ◽  
Author(s):  
Raquel Requejo ◽  
Thomas R. Hurd ◽  
Nikola J. Costa ◽  
Michael P. Murphy
Keyword(s):  
Oxidative Damage ◽  
Cysteine Residues ◽  
Protein Surfaces

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

Protective effect of chitooligosaccharides on hydrogen peroxide-induced PC-12 cells death by inhibition of oxidative damage

2010 ◽  
Vol 34 (8) ◽  
pp. S27-S27
Author(s):  
Xueling Dai ◽  
Ping Chang ◽  
Ke Xu ◽  
Changjun Lin ◽  
Hanchang Huang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidative Damage ◽  
Protective Effect ◽  
Pc 12 Cells ◽  
Cells Death

Aging and Oxidative Damage: Are Telomeres the Target?

2002 ◽  
Vol 7 (5) ◽  
pp. 295-313 ◽  
Author(s):  
Patricia A. McChesney ◽  
Lynne W. Elmore ◽  
Shawn E. Holt
Keyword(s):  
Oxidative Damage

Melatonin reduces high levels of lipid peroxidation induced by potassium iodate in porcine thyroid

2019 ◽  
pp. 1-7 ◽  
Author(s):  
Paulina Iwan ◽  
Jan Stepniak ◽  
Malgorzata Karbownik-Lewinska
Keyword(s):  
Lipid Peroxidation ◽  
Oxidative Damage ◽  
Membrane Lipids ◽  
Chemical Properties ◽  
Iodine Concentration ◽  
Free Radical Scavenger ◽  
Radical Scavenger ◽  
Protective Effects ◽  
Potassium Iodate ◽  
Hormone Synthesis

Abstract. Iodine is essential for thyroid hormone synthesis. Under normal iodine supply, calculated physiological iodine concentration in the thyroid is approx. 9 mM. Either potassium iodide (KI) or potassium iodate (KIO3) are used in iodine prophylaxis. KI is confirmed as absolutely safe. KIO3 possesses chemical properties suggesting its potential toxicity. Melatonin (N-acetyl-5-methoxytryptamine) is an effective antioxidant and free radical scavenger. Study aims: to evaluate potential protective effects of melatonin against oxidative damage to membrane lipids (lipid peroxidation, LPO) induced by KI or KIO3 in porcine thyroid. Homogenates of twenty four (24) thyroids were incubated in presence of either KI or KIO3 without/with melatonin (5 mM). As melatonin was not effective against KI-induced LPO, in the next step only KIO3 was used. Homogenates were incubated in presence of KIO3 (200; 100; 50; 25; 20; 15; 10; 7.5; 5.0; 2.5; 1.25 mM) without/with melatonin or 17ß-estradiol. Five experiments were performed with different concentrations of melatonin (5.0; 2.5; 1.25; 1.0; 0.625 mM) and one with 17ß-estradiol (1.0 mM). Malondialdehyde + 4-hydroxyalkenals (MDA + 4-HDA) concentration (LPO index) was measured spectrophotometrically. KIO3 increased LPO with the strongest damaging effect (MDA + 4-HDA level: ≈1.28 nmol/mg protein, p < 0.05) revealed at concentrations of around 15 mM, thus corresponding to physiological iodine concentrations in the thyroid. Melatonin reduced LPO (MDA + 4-HDA levels: from ≈0.97 to ≈0,76 and from ≈0,64 to ≈0,49 nmol/mg protein, p < 0.05) induced by KIO3 at concentrations of 10 mM or 7.5 mM. Conclusion: Melatonin can reduce very strong oxidative damage to membrane lipids caused by KIO3 used in doses resulting in physiological iodine concentrations in the thyroid.

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