Abstract
Peroxidized cardiolipin (diphosphatidylglycerol) reacts covalently with albumin. Incubation of albumin with increasing amounts of peroxidized cardiolipin produces a gradual increase in molecular size. Incubation with a small amount of peroxidized cardiolipin (molar ratio of cardiolipin/albumin 21) produces a mixture of complexes that differs considerably with respect to the number of cardiolipin molecules bound per molecule of albumin. With larger amounts of peroxidized cardiolipin (molar ratios of cardiolipin/albumin 54 and 114), the complexes formed seem to be of a more uniform type since the numbers of cardiolipin molecules bound per molecule of albumin are similar. No polymerization occurs for reactions in which up to at least 15 moles of cardiolipin have become bound per mole of albumin, and 20–25 moles may be bound with only very little polymerization. Only when the ratio of peroxidized cardiolipin to albumin was increased to a high value of 314 did polymerization occur. The present findings show that extensive covalent binding of peroxidized cardiolipin to albumin can occur without intermolecular crosslinking of the protein.
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Nielsen, H. Reaction between peroxidized phospholipid and protein: II. Molecular weight and phosphorus content of albumin after reaction with peroxidized cardiolipin. Lipids 14, 900–906 (1979). https://doi.org/10.1007/BF02533503
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DOI: https://doi.org/10.1007/BF02533503