Rat liver glutathione peroxidase: Purification and study of multiple forms

Fred H. Stults*, John W. Forstrom, Danny T.Y. Chiu, Al L. Tappel

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

67 Scopus citations

Abstract

The subcellular distributions of glutathione peroxidase and 75Se in rat liver were determined. Approximately 75% of the enzyme and 58% of the 73Se were contained in the cytosolic fraction. Rat liver cytosol glutathione peroxidase was purified 1029-fold from homogenate to yield a sample with a specific activity of 278 μmol of NADPH oxidized/ min/mg of protein. The purified enzyme was subjected to disc-gel and sodium dodecyl sulfate-disc-gel electrophoresis, which confirmed the purity of the enzyme as well as the existence of multiple electrophoretic forms. Glutathione peroxidase existed as a large aggregate after homogenization, and means of dissociating the aggregate were investigated. The enzyme was isolated as a neutrally charged protein and became negatively charged upon storage, a phenomenon that was independent of the aggregation.

Original languageEnglish
Pages (from-to)490-497
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume183
Issue number2
DOIs
StatePublished - 10 1977
Externally publishedYes

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