Malondialdehyde-containing proteins and their relationship to vitamin E

John D. Manwaring, A. Saari Csallany

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

A high molecular weight (Sephadex G-15 void volume), water-soluble, fluorescent material that was found to increase significantly in the mouse liver in response to vitamin E deficiency was separated into six proteins by high performance liquid chromatography (HPLC) using a TSK G2000 SW column. One of these proteins increased significantly in concentration due to vitamin E deficiency and had a molecular weight of 20,000 daltons. This protein was found to contain malondialdehyde, an end product of lipid peroxidation, attached to it presumably in a Schiff-base type structure with amino groups. This appears to be the first report in the literature of direct evidence that malondialdehyde is attached to protein in vivo.

Original languageEnglish (US)
Pages (from-to)651-655
Number of pages5
JournalLipids
Volume23
Issue number7
DOIs
StatePublished - Jul 1 1988

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