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Prevention Against Oxidative Stress of Eukaryotic Cell Membranes by Selenium Compounds of the Rat
Author(s) -
KYRIAKOPOULOS A,
BUKALIS K,
ROETHLEIN D,
HOPPE B,
GRAEBERT A,
BEHNE D
Publication year - 2004
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1329.057
Subject(s) - selenoprotein , cytosol , biochemistry , chemistry , gpx1 , selenium , cell fractionation , selenocysteine , glutathione peroxidase , enzyme , microbiology and biotechnology , glutathione , biology , organic chemistry , cysteine
A bstract : By a combination of trace techniques and various biochemical methods, information about the characteristics of a 15‐kDa selenoprotein was obtained. After labeling of rats in vivo with [ 75 Se]selenite, subcellular fractionation of the homogenates of the prostate, lung, brain, thyroid gland, and large intestine, and gel electrophoretic separation of the proteins and subcellular fractionation, 15‐kDa 75 Se was found in the cytosols of the tissues prostate > brain > lung > thyroid gland > large intestine after autoradiography. After coelectrophoresis of the separated 15‐kDa labeled band obtained from each cytosolic fraction, the 15‐kDa 75 Se band migrated in the same way as the combined bands isolated from the five tissue cytosols. After proteolytic cleavage in the gel of the 15‐kDa labeled band obtained from the cytosol of each tissue and re‐electrophoresis, the same labeled peptide pattern was found in each gel slice after autoradiography. By means of reversed‐phase HPLC, we characterized a selenocysteine‐containing protein that has enzymatic activity like that of glutathione peroxidase.