Antioxidant and Electron Donating Function of Hypothalamic Polypeptides: Galarmin and Gx-NH2

Tavadyan, L. A.; Galoian, Karina; Harutunyan, L. A.; Tonikyan, Hakob G.; Galoyan, A. A.

doi:10.1007/s11064-010-0173-8

Cited by 9 publications

(3 citation statements)

References 20 publications

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“…Turmeric is one of the famous traditional medicinal herbs which show anti-oxidant effect. Normally, the antioxidant activity of natural products is due to the presence of substituted groups such as carboxyl group, electron withdrawing group, and electron donating group in their aromatic ring structure [39]. Since the two methoxy (electron donating) groups were removed from curcumin, BDMC might show a significant electrochemical difference from the curcumin.…”

Section: Discussionmentioning

confidence: 99%

Barrier protective activities of curcumin and its derivative

Kim¹,

Lee

et al. 2012

Inflamm. Res.

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Section: Discussionmentioning

confidence: 99%

Barrier protective activities of curcumin and its derivative

Kim¹,

Lee

et al. 2012

Inflamm. Res.

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“…Under acidic conditions, proton (H + ) can compete as an electron-donating group with the metal ion, which is not likely to form a chelate. Under alkaline conditions, hydroxyl group (-OH) can also compete as an electron-donating group with the metal ion and form a hydroxide precipitate, which hinders the formation of chelates (26,27). As shown in Fig.…”

Section: The Optimal Methods Of Iron(ii)-oligopeptide Chelate Preparationmentioning

confidence: 99%

Preparation, Identification and Antioxidant Properties of Black-Bone Silky Fowl (Gallus gallus domesticus Brisson) Oligopeptide-Chelated Ferrous Iron

Pan¹,

Song²,

et al. 2016

Food Technol. Biotechnol.

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Approximately 700 million people suff er from iron deficiency of diff erent degrees, many of whom are women, children and the elderly (1). In developing countries, the situation is worse, 97 % of deaths caused by IDA occur in low-and middle-income countries (2 SummaryBlack-bone silky fowl iron(II)-oligopeptide chelate was synthesized from iron(II) solution and the black-bone silky fowl oligopeptide, which was extracted from the muscle protein of black-bone silky fowl (Gallus gallus domesticus Brisson). Orthogonal array analysis was used to determine the optimal conditions for the iron(II)-oligopeptide chelate preparation. Ultraviolet-visible (UV-Vis) spectroscopy, electron microscopy, and Fourier transform infrared (FTIR) spectroscopy were used to identify the structure of iron(II)-oligopeptide chelate. 2-Diphenyl-1-picrylhydrazyl (DPPH) and superoxide radical scavenging assays were performed to compare the antioxidant abilities of the black-bone silky fowl oligopeptide and iron(II)-oligopeptide chelate. The optimal conditions for iron(II)-oligopeptide chelate preparation were 4 % of the black-bone silky fowl oligopeptide and a ratio of the black --bone silky fowl oligopeptide to FeCl 2 ·4H 2 O of 5:1 at pH=4. Under these conditions, the chelation rate was (84.9±0.2) % (p<0.05), and the chelation yield was (40.3±0.1) % (p<0.05). The structures detected with UV-Vis spectroscopy, electron microscopy and FTIR spectra changed signifi cantly aft er chelation, suggesting that Fe(II) ions formed coordinate bonds with carboxylate (-RCOO¯) and amino (-NH 2 ) groups in the oligopeptides, confi rming that this is a new oligopeptide-iron chelate. The iron(II)-oligopeptide chelate had stronger scavenging activity towards DPPH and superoxide radicals than did the black-bone silky fowl oligopeptide.

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“…PRP-1 also possess immunotrop and neuroprotective properties [11]. It was shown recently that PRP-1 is capable of neutralizing highly active hydroxy radicals (HO ÁÁÁ ) [23], which in their turn inactivate MAA and MPA, thus through that route PRP-1 normalizes the MAA (Cu, Zn-SOD, catalase and ceruloplasmin) and MPA to norm during different pathological states. Moreover, it increases NADPH dependent O 2 -producing and ferriHb-reducing activities of MPA in vitro and in vivo [19,20].…”

Section: Introductionmentioning

confidence: 99%

Proline Rich Polypeptide (PRP-1) Increases the Superoxide-Producing and Ferrihemoglobin Reducing Activities of Cytochrome B558 Isoforms from Human Lymphosarcoma Tissue Cells

Simonyan¹,

Galoian

Simonyan³

et al. 2011

Neurochem Res

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The two cytochromes (cyt) b(558) of acidic nature, one-95-100 kDa and another one, 60-70 kDa were isolated for the first time from the human's lymphosarcoma tissue cells using gel filtration and ion exchange chromatography. These hemoproteins possess NADPH dependent O(2)(-)-producing and ferrihemoglobin-reducing activities. The incubation of neuropeptide PRP-1 (5 μg) with cytochrome b(558), caused elevation of these activities. The gel filtration results indicated possible binding of PRP-1 to these cytochromes b(558). PRP-1 activated both NADPH dependent O(2)(-)-producing and ferriHb-reducing activities of the cyt b(1)(558) and cyt b(2)(558), obtained from human lymphosarcoma tissue cells. One can assume that PRP-1 associated with cyt b(558) on the surface of the tumor cells by increasing both NADPH dependent O(2)(-)-producing and ferriHb-reducing activities of cyt b(558), increases the oxidation- reduction status. Changing the oxidation-reduction status and oxygen homeostasis of the tumor cells by PRP-1 can serve as one of the possible explanation of antitumorigenic effect of this cytokine.

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Antioxidant and Electron Donating Function of Hypothalamic Polypeptides: Galarmin and Gx-NH2

Cited by 9 publications

References 20 publications

Barrier protective activities of curcumin and its derivative

Barrier protective activities of curcumin and its derivative

Preparation, Identification and Antioxidant Properties of Black-Bone Silky Fowl (Gallus gallus domesticus Brisson) Oligopeptide-Chelated Ferrous Iron

Proline Rich Polypeptide (PRP-1) Increases the Superoxide-Producing and Ferrihemoglobin Reducing Activities of Cytochrome B558 Isoforms from Human Lymphosarcoma Tissue Cells

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