Selenium, glutathione peroxidase and other selenoproteins

Thesis/Dissertation · Sat Jan 01 04:00:00 EST 1983

OSTI ID:6101318

Wilhelmsen, E C

Selenium, as essential trace element, has long been associated with protein. The essentiality of selenium is partially understood as glutathione peroxidase contains an essential selenocysteine. Glutathione peroxidase has been purified from many tissues including rat liver. An estimated molecular weight of 105,000 was obtained for glutathione peroxidase by comparison to standards. A subunit size of 26,000 was obtained by SDS-gel electrophoresis. Glutathione peroxidase is not the only selenoprotein in the rat. In seven rat tissues examined, there were many different subunit sizes and change groups representing between 9 and 23 selenoproteins. Selenocysteine in glutathione peroxidase accounts for ca. 36% of the selenium in the rat. The mode of synthesis of glutathione peroxidase and the other selenoproteins is not understood. Glutathione peroxidase is strongly and reversibly inhibited by mercaptocarboxylic acids and other mercaptans, including some used as slow-acting drugs for the symtomatic treatment of rheumatoid arthritis. The mechanism and chemistry of this inhibition is discussed. This inhibition may provide a link between selenium and arthritis.

• OSTI ID: 6101318
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
BIOSYNTHESIS
BODY
CARBOXYLIC ACIDS
DIGESTIVE SYSTEM
DISTRIBUTION
DRUGS
ELEMENTS
ENZYME INHIBITORS
ENZYMES
GLANDS
GLUTATHIONE
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
LIVER
MAMMALS
METABOLISM
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANS
OXIDOREDUCTASES
PEPTIDES
PEROXIDASES
POLYPEPTIDES
PORPHYRINS
PROTEINS
RADIOPROTECTIVE SUBSTANCES
RATS
RODENTS
SELENIUM
SELENIUM COMPOUNDS
SEMIMETALS
SYNTHESIS
TISSUE DISTRIBUTION
VERTEBRATES