Premium
Reaction between peroxidized phospholipid and protein: I. Covalent binding of peroxidized cardiolipin to albumin
Author(s) -
Nielsen Henning
Publication year - 1978
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02533665
Subject(s) - cardiolipin , cardiolipins , albumin , chemistry , phospholipid , serum albumin , covalent bond , biochemistry , moiety , chromatography , size exclusion chromatography , organic chemistry , enzyme , membrane
A system is described for study of the reaction of peroxidized cardiolipin (diphosphatidylglycerol) with albumin. Covalent binding of peroxidized cardiolipin to albumin occurs in this system as evidenced partly by a decrease in lipid‐extractable P and partly by lipid P being inseparable from the albumin by gel filtration in the presence of a detergent (sodium deoxycholate) under conditions known to separate the lipid moiety and apoprotein of lipoproteins. Based on analyses of the decrease in lipid‐extractable P, the average number of cardiolipin molecules bound covalently per molecule of albumin is about 5 when peroxidized cardiolipin (4 moles O 2 /mol cardiolipin) at about 10 times molar excess is allowed to react with albumin. However, the data of the gel filtration experiment indicate that the bound peroxidized cardiolipin molecules may not be evenly distributed on the albumin molecules. Therefore, the number of cardiolipin molecules bound per albumin molecule may actually vary over a range and be considerably higher for part of the albumin. The findings have been discussed in relation to peroxidation in vivo.