Literature DB >> 2484406

Role of glutathione in selenite binding by human plasma.

A Mas1, B Sarkar.   

Abstract

The erythrocyte-mediated reduction of selenite has been reproduced by the addition of reduced glutathione to plasma at levels comparable to those present in the erythrocyte. The reaction has been followed by chromatography and ultraviolet (UV) absorption spectroscopy (in the absence of plasma). The first detectable compound, selenium diglutathione, is very unstable in physiological conditions. The product of the reaction does not contain glutathione and is able to react and incorporate selenium into plasma proteins without the participation of hemoglobin or glutathione reductase. A saturable low molecular weight compound is also able to bind selenium, which may be relevant in the initial distribution and excretion of selenium after selenite administration.

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Year:  1989        PMID: 2484406     DOI: 10.1007/bf02919102

Source DB:  PubMed          Journal:  Biol Trace Elem Res        ISSN: 0163-4984            Impact factor:   3.738


  22 in total

1.  Reduction of disulfide-containing amines amino acids, and small peptides.

Authors:  J Bulter; S P Spielberg; J D Schulman
Journal:  Anal Biochem       Date:  1976-10       Impact factor: 3.365

2.  Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine.

Authors:  W Leinfelder; E Zehelein; M A Mandrand-Berthelot; A Böck
Journal:  Nature       Date:  1988-02-25       Impact factor: 49.962

3.  Reduction of the selenotrisulfide derivative of glutathione to a persulfide analog by glutathione reductase.

Authors:  H E Ganther
Journal:  Biochemistry       Date:  1971-10-26       Impact factor: 3.162

4.  The metabolism of selenite in cow blood in vitro.

Authors:  M Sandholm
Journal:  Acta Pharmacol Toxicol (Copenh)       Date:  1973

5.  Metabolism of 75Se-selenite by human whole blood in vitro.

Authors:  M Lee; A Dong; J Yano
Journal:  Can J Biochem       Date:  1969-08

6.  Acid-volatile selenium formation catalyzed by glutathione reductase.

Authors:  H S Hsieh; H E Ganther
Journal:  Biochemistry       Date:  1975-04-22       Impact factor: 3.162

7.  Reaction of selenium with immunoglobulin molecules.

Authors:  R M Burton; P J Higgins; K P McConnell
Journal:  Biochim Biophys Acta       Date:  1977-08-23

8.  Selenium: biochemical role as a component of glutathione peroxidase.

Authors:  J T Rotruck; A L Pope; H E Ganther; A B Swanson; D G Hafeman; W G Hoekstra
Journal:  Science       Date:  1973-02-09       Impact factor: 47.728

9.  Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine.

Authors:  J W Forstrom; J J Zakowski; A L Tappel
Journal:  Biochemistry       Date:  1978-06-27       Impact factor: 3.162

10.  Periodate-oxidized adenosine inhibits the formation of dimethylselenide and trimethylselenonium ion in mice treated with selenite.

Authors:  J L Hoffman; K P McConnell
Journal:  Arch Biochem Biophys       Date:  1987-05-01       Impact factor: 4.013

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  3 in total

1.  Chemical form of selenium-containing metabolite in small intestine and liver of mice following orally administered selenocystine.

Authors:  T Hasegawa; M Mihara; T Okuno; K Nakamuro; Y Sayato
Journal:  Arch Toxicol       Date:  1995       Impact factor: 5.153

2.  Effect of selenium compounds on murine B16 melanoma cells and pigmented cloned pB16 cells.

Authors:  B Siwek; E Bahbouth; M A Serra; E Sabbioni; M C de Pauw-Gillet; R Bassleer
Journal:  Arch Toxicol       Date:  1994       Impact factor: 5.153

Review 3.  Understanding the Redox Biology of Selenium in the Search of Targeted Cancer Therapies.

Authors:  Jeffrey M Stolwijk; Rohan Garje; Jessica C Sieren; Garry R Buettner; Yousef Zakharia
Journal:  Antioxidants (Basel)       Date:  2020-05-13
  3 in total

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