|
|
 Previous Article | Table of Contents | Next Article 
Selenium-dependent glutathione peroxidase protein and activity:
immunological investigations on cellular and plasma enzymes
K Takahashi and HJ Cohen
Selenium-deficient humans and animals are known to be deficient in
glutathione peroxidase (GSHPx) activity in their cells and plasma. To
determine the relationship between enzyme activity and protein content, the
enzyme was purified from human erythrocytes, and polyclonal antibodies were
made against the purified protein in rabbits. These antibodies were found
to be monospecific, noninhibitory, and capable of precipitating the
enzymatic activity. All the GSHPx activity in erythrocytes and almost all
the activity in neutrophils and platelets was precipitated by these
antibodies. None of the plasma enzyme was precipitated by these antibodies,
indicating that the plasma enzyme activity was attributable to a different
selenium dependent protein moiety. Utilizing a radioimmunoassay, we were
able to determine that there was a direct relationship between GSHPx
activity and protein content in the erythrocytes of both normal and
selenium-deficient individuals, and a similar relationship between control
and selenium- deficient rat erythrocytes and liver cells. Thus, the ability
to examine GSHPx as a protein resulted in two new observations concerning
the selenium-dependent GSHPx. The first is that the plasma enzyme is
antigenically distinct from the erythrocyte enzyme, and the second is that
in the absence of selenium, there is a concomitant decrease in GSHPx
protein.
Volume 68,
Issue 3,
pp. 640-645,
09/01/1986
Copyright © 1986 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
J. C. Whitin, S. Bhamre, D. M. Tham, and H. J. Cohen
Extracellular glutathione peroxidase is secreted basolaterally by human renal proximal tubule cells
Am J Physiol Renal Physiol,
July 1, 2002;
283(1):
F20 - F28.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
I S Young and J V Woodside
Antioxidants in health and disease
J. Clin. Pathol.,
March 1, 2001;
54(3):
176 - 186.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y. Saito, T. Hayashi, A. Tanaka, Y. Watanabe, M. Suzuki, E. Saito, and K. Takahashi
Selenoprotein P in Human Plasma as an Extracellular Phospholipid Hydroperoxide Glutathione Peroxidase. ISOLATION AND ENZYMATIC CHARACTERIZATION OF HUMAN SELENOPROTEIN P
J. Biol. Chem.,
January 29, 1999;
274(5):
2866 - 2871.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Schnurr, A. Borchert, and H. Kuhn
Inverse regulation of lipid-peroxidizing and hydroperoxyl lipid-reducing enzymes by interleukins 4 and 13
FASEB J,
January 1, 1999;
13(1):
143 - 154.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
A. K. Singh and H. Shichi
A Novel Glutathione Peroxidase in Bovine Eye. SEQUENCE ANALYSIS, mRNA LEVEL, AND TRANSLATION
J. Biol. Chem.,
October 2, 1998;
273(40):
26171 - 26178.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Q. Shen, R. Wu, J. L. Leonard, and P. E. Newburger
Identification and Molecular Cloning of a Human Selenocysteine Insertion Sequence-binding Protein. A BIFUNCTIONAL ROLE FOR DNA-BINDING PROTEIN B
J. Biol. Chem.,
March 6, 1998;
273(10):
5443 - 5446.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
X. G. Lei, H. M. Dann, D. A. Ross, W.-H. Cheng,, G. F. Combs Jr., and K. R. Roneker
Dietary Selenium Supplementation Is Required to Support Full Expression of Three Selenium-Dependent Glutathione Peroxidases in Various Tissues of Weanling Pigs
J. Nutr.,
January 1, 1998;
128(1):
130 - 135.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
W.-H. Cheng, Y.-S. Ho, D. A. Ross, B. A. Valentine, G. F. Combs Jr., and X. G. Lei
Cellular Glutathione Peroxidase Knockout Mice Express Normal Levels of Selenium-Dependent Plasma and Phospholipid Hydroperoxide Glutathione Peroxidases in Various Tissues
J. Nutr.,
August 1, 1997;
127(8):
1445 - 1450.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
W.-H. Cheng, Y.-S. Ho, D. A. Ross, Y. Han, G. F. Combs Jr., and X. G. Lei
Overexpression of Cellular Glutathione Peroxidase Does Not Affect Expression of Plasma Glutathione Peroxidase or Phospholipid Hydroperoxide Glutathione Peroxidase in Mice Offered Diets Adequate or Deficient in Selenium
J. Nutr.,
May 1, 1997;
127(5):
675 - 680.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Schnurr, J. Belkner, F. Ursini, T. Schewe, and H. Kühn
The Selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase Controls the Activity of the 15-Lipoxygenase with Complex Substrates and Preserves the Specificity of the Oxygenation Products
J. Biol. Chem.,
March 1, 1996;
271(9):
4653 - 4658.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
