Glutathione, Cysteine, and D-Penicillamine Role in Exchange of Silver Metal from the Albumin Metal Complex.

The purpose of this study is to investigate the exchange reaction taking place among the bovine serum albumin (BSA), 5,5 ′ -dithiobis-(2-nitrobenzoic acid (ESSE), reduced glutathione, N-acetylcysteine, D-penicillamine (thiolates), and silver metal (AgI). For this purpose, stock solutions of BSA and...

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Publicado en:BioMed Research International pp. 1 - 11
Autores principales: Alharthi, Nahed S., Khan, Haroon, Siyal, Fahad Jibran, Shaikh, Zahid Ali, Arain, Shumaila Parveen, Eltayeb, Lienda Bashier, Mangi, Altaf Ali
Formato: equations & formulas pictorial research tables/charts Journal Article
Publicado: Wiley-Blackwell 8/8/2022
Acceso en línea:Ver este registro en EBSCOhost
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      dt: 8/8/2022
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      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        10.1155/2022/3619308
        158405585
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        atl: Glutathione, Cysteine, and D-Penicillamine Role in Exchange of Silver Metal from the Albumin Metal Complex.
      aug:
        au:
          Alharthi, Nahed S.
          Khan, Haroon
          Siyal, Fahad Jibran
          Shaikh, Zahid Ali
          Arain, Shumaila Parveen
          Eltayeb, Lienda Bashier
          Mangi, Altaf Ali
        affil: Department of Medical Laboratory Sciences, College of Applied Medical Sciences, Prince Sattam Bin Abdulaziz University, Al-Kharj 11942, Saudi Arabia
      sug:
        subj:
          Glutathione Blood
          Cysteine Blood
          Penicillamine Blood
          Silver Blood
          Serum Albumin Metabolism
          Animal Studies
          Cattle
          Spectrophotometers
          Molecular Structure
          Indicators and Reagents
          Buffers
          Chromatography
          Oxidation-Reduction
      ab: The purpose of this study is to investigate the exchange reaction taking place among the bovine serum albumin (BSA), 5,5 ′ -dithiobis-(2-nitrobenzoic acid (ESSE), reduced glutathione, N-acetylcysteine, D-penicillamine (thiolates), and silver metal (AgI). For this purpose, stock solutions of BSA and Ellman's reagent were prepared by dissolving 264 mg of BSA in 5 ml of reaction buffer (0.1 M KH2PO4 at pH 7.8) and 23.8 mg of ESSE in 1.0 ml of reaction buffer which were mixed together. Mixture of BSA-AgI was prepared in a separate procedure by dissolving 0.17 mg of silver nitrate in 1 ml of reaction buffer and then dissolving BSA (200 mg) in the same solution of silver nitrate. Blocking of Cys-34 of BSA with AgI was confirmed by treating different dilutions of BSA-AgI (500 μM) solutions with the solutions of ESSE (85 μM) and ES- (85 μM) and recording the spectra (300-450) with a UV-visible spectrophotometer. The chromatographed AgI-modified BSA ((BSA-S)AgI)) samples (typically 500 μM) were subsequently mixed with thiolates (reduced glutathione, N-acetylcysteine, and D-penicillamine). AgI and modified BSA (typically 500 μM each) were treated with these low molecular weight thiolates and allowed to react overnight followed by chromatographic separation (Sephadex G25). The redox reactions of AgI-modified BSA with various low molecular weight thiols revealed a mechanically important phenomenon. In the case of reduced glutathione and N-acetylcysteine, we observed the rapid release of a commensurate amount of Ellman's anion, indicating that an exchange has taken place and low molecular weight thiols (RSH) substituted AgI species at the Cys-34 of BSA eventually forming disulfide (BSA-SSR) at Cys-34. It can be anticipated from the phase of study involving bovine serum albumin that low molecular weight thiolates (reduced glutathione and N-acetylcysteine) take off AgI which are attached to proteins elsewhere in the physiological system, making these toxic metals free for toxic action.
      pubtype: Academic Journal
      doctype:
        equations & formulas
        pictorial
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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