Cited by 885Selenium in Biological SystemsRedox biology and oxidative stressAntioxidant Activity and Oxidative Stress

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Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides

Ursini, F., Maiorino, M., Valente, M., Ferri, L., Gregolin, C.·1982·Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism

DOI 10.1016/0005-2760(82)90150-3

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Abstract

The cell sap from pig liver contains a protein which protects phosphatidylcholine liposomes and biomembranes from peroxidative degradation in the presence of glutathione. The activity of this protein has been assayed by measuring the inhibition of aged phosphatidylcholine liposome peroxidation induced by the Fe3+-triethylenetetramine complex. The peroxidation-inhibiting protein from pig liver has been purified 585-fold to homogeneity with overall recovery of activity of 12%. (NH4)2SO4 precipitation, ion-exchange chromatography on DEAE-Sepharose CL-6B and CM23-cellulose, affinity chromatography on glutathione-bromosulfophthalein-Sepharose and gel filtration on Sephadex G-50 were used. Gel filtration and SDS- polyacrylamide gel electrophoresis indicated a molecular weight of approximately 20 000. The protein inhibited peroxidation by Fe3+-triethylenetetramine following a 15 min preincubation of phosphatidylcholine liposomes in the presence of 5mM glutathione or 2-mercapthoethanol. The pure protein exhibited glutathione peroxidase activity on hydroperoxide groups of phosphatidylcholine and on cumene and t-butyl hydroperoxides, with specific activities of 2.2, 3.8 and 0.9 mumol/min per mg protein, respectively. The protein appears to be distinct from the selenoenzyme glutathione peroxidase and from any known glutathione S-transferase. The peroxidation was studied also with fresh phosphatidylcholine liposomes and was induced in this case by Fe-ascorbate. To obtain protection by the peroxidation-inhibiting protein and glutathione, preincubation was not necessary, but alpha-tocopherol, incorporated in the liposomes in the molar ratio 1:250 to phosphatidylcholine, was required. Lipid peroxidation of rat liver mitoplasts and microsomes was blocked when these preparations were incubated in the peroxidizing mixture in the presence of peroxidation-inhibiting protein and glutathione. The protection from Fe3+-triethylenetetramine-induced peroxidation is related apparently to reduction of hydroperoxide groups in polyunsaturated fatty acid residues of phospholipids and to inhibition of free radicals formation by chain branching. Protection from the Fe-ascorbate-induced peroxidation is apparently attributable to the same mechanism. However, the requirement of alpha-tocopherol for protection in the Fe-ascorbate-induced peroxidation suggests that the cooperation of a free-radical scavenger is necessary. It is probable that the glutathione peroxidase activity is involved also in the glutathione-dependent protection exhibited by the protein on lipid peroxidation of biomembranes.

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Authors: Ursini, F., Maiorino, M., Valente, M., Ferri, L., & Gregolin, C.
Affiliations: University of Padua (IT)
ORCID: Ursini, F.
Maiorino, M.
Valente, M.
Gregolin, C.
Venue: Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
Publisher: Elsevier BV
Published: 1982-02
Volume: 710
Issue: 2
Pages: 197-211
ISSN: 0005-2760 (ISSN-L)
DOI: 10.1016/0005-2760(82)90150-3
OpenAlex: W1966920840
Cited by: 884
References: 25
Citations by year: 2026: 42 · 2025: 68 · 2024: 81 · 2023: 69 · 2022: 63 · 2021: 46 · 2020: 37 · 2019: 17 · 2018: 16 · 2017: 18 · 2016: 15 · 2015: 13 · 2014: 11 · 2013: 13 · 2012: 17
FWCI: 12.85
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism (publishedVersion)
PubMed (publishedVersion)
Padua Research Archive (University of Padova) (submittedVersion)
Funders: Regione del Veneto
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Keywords: glutathione peroxidase activity, phosphatidylcholine liposomes, lipid peroxidation, glutathione, porcine liver, protein purification, triethylenetetramine, alpha-tocopherol, liver microsomes, hydroperoxide reduction, antioxidant enzymes, glutathione S-transferase, cumene hydroperoxide
MeSH terms: Animals, Glutathione Peroxidase, Kinetics, Lipid Peroxides, Liposomes, Liver, Membranes, Peroxidases, Peroxides, Phosphatidylcholines, Proteins, Subcellular Fractions, Swine

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Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides

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