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Complexes were formed between egg albumin and oxidized lipids, such as thermally oxidized corn oil and autoxidized linoleic acid, under a standardized set of conditions. No complex could be obtained under these conditions when lysine, glycine, bactopeptone, gelatin or sodium caseinate were substituted for egg albumin. Lactalbumin was equally as reactive, casein much less and fresh egg white superior to egg albumin in their complexing ability with oxidized corn oil. As the time of reaction was increased, the amount of the complex formed also increased. Optimum complex formation took place at a concentration of 1% protein, a pH of 7 and 60C. The ease of formation of these complexesin vitro indicated that similar complexing could readily take placein vivo under suitable pathological conditions.
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Narayan et al. (1963) studied this question.
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