title: Role of glutathione in selenite binding by human plasma.
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.
authors.affiliation: Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.
authors.forename: A
authors.initials: A
authors.lastname: Mas
authors.forename: B
authors.initials: B
authors.lastname: Sarkar
mesh_terms: D001798:Blood Proteins / Q000378:metabolism; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D004912:Erythrocytes / Q000378:metabolism; D005978:Glutathione / Q000502:physiology*; D005980:Glutathione Reductase / Q000097:blood; D006801:Humans; D066298:In Vitro Techniques; D020887:Selenious Acid; D012643:Selenium / Q000097:blood*; D012644:Selenium Radioisotopes; D013056:Spectrophotometry, Ultraviolet
chemical_list: D001798:Blood Proteins; D012644:Selenium Radioisotopes; D005980:Glutathione Reductase; D020887:Selenious Acid; D005978:Glutathione; D012643:Selenium