Faculty Collaboration Database

Superoxide and hydrogen peroxide-dependent lipid peroxidation in intact and triton-dispersed erythrocyte membranes. Biochem Biophys Res Commun 1984 Jan 30;118(2):474-80

Date

01/30/1984

Pubmed ID

6322749

DOI

10.1016/0006-291x(84)91327-5

Scopus ID

2-s2.0-0021366055 (requires institutional sign-in at Scopus site)   69 Citations

Abstract

Isolated erythrocyte membranes incubated with xanthine, xanthine oxidase, and Fe(III) underwent lipid peroxidation, as indicated by the thiobarbituric acid reaction and iodometric determination of hydroperoxides. In detergent-free medium (phosphate buffered saline) peroxidation was inhibited by superoxide dismutase, catalase, and EDTA; but was promoted by OH. scavangers, eg. mannitol. Generation of OH. in the system via iron-catalyzed reduction of H2O2 by O-2 was demonstrated by EPR spectrometry using spin trapping. In membranes treated with Triton X-100 lipid peroxidation was stimulated by EDTA and suppressed by OH. traps. This and other evidence suggests that OH. in the medium was an effective initiator of lipid peroxidation in detergent-dispersed membranes, but not in intact membranes.

Author List

Girotti AW, Thomas JP

Authors

Albert Girotti PhD, MS Emeritus Professor in the Biochemistry department at Medical College of Wisconsin
James P. Thomas PhD, MD Professor in the Medicine department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Catalase
Edetic Acid
Erythrocyte Membrane
Humans
Hydrogen Peroxide
Kinetics
Lipid Peroxides
Mannitol
Superoxide Dismutase
Superoxides