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.
Manwaring
J D
JD
University of Minnesota, Department of Food Science and Nutrition, St. Paul 55108.
Csallany
A S
AS
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