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Antihuman plasma glutathione peroxidase antibodies: immunologic
investigations to determine plasma glutathione peroxidase protein and
selenium content in plasma
N Avissar, JC Whitin, PZ Allen, IS Palmer and HJ Cohen
Department of Pediatrics, University of Rochester, School of Medicine and
Dentistry, NY 14642.
Plasma glutathione peroxidase (GSHPx) (glutathione: H2O2 oxidoreductase) is
a unique selenoglycoprotein. Treatment of this enzyme with glycopeptidase F
partially deglycosylates it and establishes the presence of N-linked sugar
moieties. Antibodies raised in a rabbit against the purified enzyme from
plasma were found to be specific, noninhibitory, and capable of
precipitating the enzymatic activity. The antibodies precipitated greater
than 90% of the GSHPx activity of normal plasma, thus indicating that the
selenoenzyme is the main if not the sole GSHPx activity of plasma. The
antibodies did not precipitate RBC GSHPx. A slight cross-reactivity of the
antibodies was found with rat plasma GSHPx. A GSHPx activity precipitation
assay of normal plasma in the presence of selenium (Se)-deficient plasma
indicates that no cross-reactive protein in the Se-deficient plasma
interferes with the precipitation of the GSHPx activity from normal plasma.
Thus, GSHPx protein as well as activity is deficient in plasma in the
absence of Se. Antibodies against GSHPx either from RBCs or from plasma
were used to specifically immunoprecipitate most of the GSHPx activity from
RBCs or plasma, respectively, in healthy individuals to determine the
amount of Se associated with the protein. GSHPx accounts for approximately
15% of the Se in RBCs and 12% of the Se in plasma. Thus, in normal
individuals, these proteins account for only a fraction of plasma and RBC
Se.
Volume 73,
Issue 1,
pp. 318-323,
01/01/1989
Copyright © 1989 by The American Society of Hematology
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