Malondialdehyde-containing proteins and their relationship to vitamin E.
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.
University of Minnesota, Department of Food Science and Nutrition, St. Paul 55108.
J D
JD
Manwaring
A S
AS
Csallany
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005260:Female; D006868:Hydrolysis; D008314:Malonates / Q000032:analysis*; D008315:Malondialdehyde / Q000032:analysis*; D051379:Mice; D008810:Mice, Inbred C57BL; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*; D014811:Vitamin E Deficiency / Q000378:metabolism*
D008314:Malonates; D011506:Proteins; D008315:Malondialdehyde