Malondialdehyde‐containing proteins and their relationship to vitamin E

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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.