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Garlic
Published in Robert E.C. Wildman, Richard S. Bruno, Handbook of Nutraceuticals and Functional Foods, 2019
Sharon A. Ross, Craig S. Charron
It should be noted that not all organosulfur compounds have been found to exhibit antioxidant properties. DADS, but not DAS, dipropyl sulfide, or dipropyl disulfide, has been found to inhibit liver microsomal-lipid peroxidation induced by NADPH, ascorbate, and doxorubicin.161 The presence of both the allyl and sulfur groups appears to magnify the antioxidant capabilities of the molecule. Both the number of sulfur atoms and the oxidation state of sulfur atoms can influence the overall antioxidant potential.162 Whereas allicin is effective in retarding methyl linoleate oxidation, it is less than that caused by α-tocopherol.163 Organosulfur compounds such as SAC are recognized to be powerful antioxidants and radical scavengers with the strong capacity to minimize oxidization.160 Antioxidant activity of garlic shows great variation depending on the genotype or species evaluated for activity.164,165 Moreover, processing of garlic may affect antioxidant efficacy; the heating of garlic can not only denature proteins, but also its antioxidant properties.166
Biochemical Aspects of Nickel Hypersensitivity: Factors Determining Allergenic Action
Published in Jurij J. Hostýnek, Howard I. Maibach, Nickel and the Skin, 2019
Baldassarré Santucci, Emanuela Camera, Mauro Picardo
The nickel oxidation states vary from -1 to +4. In biological systems the soluble Ni(II), classically considered responsible for the induction of contact allergy, is the one most frequently found. It exists either in particulate form or as a coordination complex with water alone — as a green hexaquinonickel (II) ion ([Ni(H2O)6]2+) — or with water and other ligands (Coogan et al., 1989). The electrochemical reaction between metal objects and sweat leads to the formation of different amounts of Ni(II) ions in vivo. In Ni-enzymes the oxidation state of nickel is II in active dehydrogenase, hydrogenase, and urease, whereas it is I in active methyl-coenzyme M reductase (Thauer, 2001).
Phylogeny of Normal and Abnormal Hemoglobin Genes
Published in S. K. Dutta, DNA Systematics, 2019
Hemoglobin, the principal respiratory protein in all vertebrates with the possible exception of a few Antarctic fish, is a tetrameric protein consisting of two pairs of polypeptide subunits or “chains”. By convention, one pair is referred to as the a chains and the other as the non-a chains. In most animal species, when multiple normal hemoglobin types occur, one of the chains is common to all and that commonality is the distinguishing feature of the a chain. As will be discussed more extensively below, there is a marked degree of molecular homology between the a and non-a chains of a given species as well as interspecies homology between chains of like type (and obviously therefore, between unlike types as well). Each chain has associated with it a heme group which is a protoporphyrin IX group and which contains one iron atom. In functional hemoglobin, these iron atoms must be in the ferrous or 2+ oxidation state. When the iron assumes the 3+ state, the resultant hemoglobin is known as methemoglobin and is totally nonfunctional. Paradoxically then, oxygen, the principal ligand of hemoglobin, is also its worst enemy. Indeed, the internal milieu of the red cell is nearly anaerobic and one of the functions of the globin chain is the protection of the heme iron from oxidation.
Poly-β-Cyclodextrin-coated neodymium-containing copper sulphide nanoparticles as an effective anticancer drug carrier
Published in Journal of Microencapsulation, 2022
Archana Sumohan Pillai, Aleyamma Alexander, Govindaraj Sri Varalakshmi, Varnitha Manikantan, Bose Allben Akash, Israel V. M. V. Enoch
The element composition in the as-synthesised NCS NPs was investigated using EDX spectroscopy. The EDX spectrum is displayed in Figure 2(A). The spectrum shows peaks featuring elements Cu, Nd, and S, implying qualitatively the composition of the NCS NPs. Further evidence for the elemental composition and the electronic states of Cu, Nd, S, C, and O are obtained from the XPS peaks. The XPS of Cu (Figure 2(B)) reveals peaks at 932.7 and 952.77 eV, characteristic of the 2p3/2 and 2p1/2 configurations respectively (Karikalan et al.2017). The two peaks mean the oxidation state of 2. The high-resolution Nd 3d core levels of the P-NCS is revealed by the binding energies at 982.41 and 1604.87 eV (Figure 2(C)) corresponding to the 3d5/2 and 3d3/2 respectively (Kim et al.2013). Further, the S 2p spectra are deconvoluted into two components viz., 163.01 eV and 169.14 eV (Figure 2(D)). The binding energies correspond to the states of S 2p3/2 and 2p1/2 respectively. The poly-CD on the P-NCS NPs contribute to the C and O spectra. The deconvoluted spectra showing peaks at 531.39 and 533.11 eV (Figure 2(E)) represent the energy states corresponding to the C–O and the C–O–H oxygens (O 1 s). Similarly, the BE’s 284.96, 286.73, and 287.98 eV are indicative of the C–O–C, C–C, and O–C = O carbons in C 1 s states (Figure 2(F)).
Potential of Application of Iron Chelating Agents in Ophthalmic Diseases
Published in Seminars in Ophthalmology, 2021
Alireza Ghaffarieh, Joseph B. Ciolino
Iron is a critical element in the basic biochemical cycles in human physiology. Numerous proteins that have important parts in cell physiology need iron to work. A significant number of these proteins are profoundly rationed across prokaryotes and eukaryotes, and the unique situation of iron in cell digestion is kept up in practically all types of life. It is also necessary for fundamental metabolic processes, including DNA synthesis and repair, transcription, and energy production in the mitochondria.1 Insufficient intracellular iron levels impair the activity of iron-containing proteins, ultimately compromising cell function and viability. Iron’s basic role is its capability to change between oxidation states, principally between divalent ferrous (Fe2+) and trivalent ferric (Fe3+) iron.2 Iron catalyzes the production of reactive oxygen species (ROS).3 Exposure to these highly reactive radicals damages lipids, nucleic acids, and proteins, causing cell and thus tissue damage. Although iron metabolism is subject to relatively rigid physiological control, many disorders have recently been related to deregulated iron homeostasis. Because of its involvement in these diseases’ pathogenesis, iron metabolism constitutes a promising and mostly unexploited therapeutic target for developing new pharmacological treatments.
Cardioprotective effect of rosmarinic acid against myocardial ischaemia/reperfusion injury via suppression of the NF-κB inflammatory signalling pathway and ROS production in mice
Published in Pharmaceutical Biology, 2021
Wei Quan, Hui-xian Liu, Wei Zhang, Wei-juan Lou, Yang-ze Gong, Chong Yuan, Qing Shao, Na Wang, Chao Guo, Fei Liu
The body’s oxidative function can be reflected by changes in ROS. ROS determination can be used to measure oxidative tissue and cell damage (Qiu et al. 2019), and previous studies have reported that RosA has a powerful antioxidation effect. Thus, DHE-ROS was adopted to detect the oxidation state of myocardial tissue and cells. Simply stated, the DHE-ROS detection kit detects active oxygen utilizing the fluorescent probe dihydroethidium. DHE is freely accessible to the cell through the living cell membrane and is oxidized by ROS in the cell to form ethidium oxide, which can mix with chromosomal DNA to produce red fluorescence. It is possible to estimate the amount of ROS and change in its content in cells according to the red fluorescence produced in living cells (Hardy et al. 2015). Accordingly, the obtained results demonstrated that RosA could reduce ROS generation in the myocardial I/R injury area and after cell OGD/R injury. Aconitase (ACO) is an important iron-sulfur (Fe-S) protease in cells that is attacked by ROS when its Fe-S active centre undergoes I/R injury, leading to ACO oxidative inactivation (Lou et al. 2014). According to aconitase detection, RosA was found to alleviate oxidative inactivation of ACO in the myocardial I/R injury area in mice and after cell OGD/R injury. The above experiments verified that the myocardial protective effect of RosA is closely correlated with a reduction in ROS generation.