Abstract
Little is known about the posttranslational processing of glutathione peroxidase (GSH-Px)(GSH:H2O2oxidoreductase, EC 1.11.1.9). The difference of 10 amino acids in the reported position of selenocysteine in bovine erythrocyte GSH-Px, as determined by crystallographic analysis1 as compared to chemical sequence analysis,2 suggests that a polypeptide may have been cleaved from the crystallized GSH-Px. In a study of rat liver mitochondrial GSH-Px, Voight and Autor3 reported that the initial GSH-Px gene product may be as much as 5 kDa larger than the mature enzyme. These two reports thus suggest that newly synthesized GSH-Px may be processed to a smaller molecular weight form during maturation. We have been studying various aspects of GSH-Px synthesis using immunoblotting with anti-GSH-Px antibodies to measure levels of GSH-Px protein, and using SDS-gel electrophoresis to follow 75Se incorporation into selenoproteins. In the course of these studies, we have observed that GSH-Px can be detected in several forms that differ in their apparent molecular weight. The purpose of this report is to further describe these different molecular weight forms of GSH-Px.
Supported by the University of Arizona Experiment Station and NIH (AM 32942)
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© 1988 Plenum Press, New York
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Sunde, R.A., Knight, S.A.B., Geyman, T.W., Evenson, J.K. (1988). Apparent Proteolytic Modification of Glutathione Peroxidase. In: Hurley, L.S., Keen, C.L., Lönnerdal, B., Rucker, R.B. (eds) Trace Elements in Man and Animals 6. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0723-5_8
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DOI: https://doi.org/10.1007/978-1-4613-0723-5_8
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