Changes in myoglobin due to lipid oxidation were studied in a model system, consisting of a mixture of metmyoglobin and methyl linoleate (2:1), which was mechanically emulsified, freeze‐dried and stored at 37°C. After storage, samples were reconstituted, centrifuged and lipid fractions were separated and tested for degree of oxidation. The protein was recovered in two fractions: “soluble fraction” (supernatant) and “aggregates” (precipitated proteins). Absorption spectroscopy confirmed protein insolubilization due to formation of aggregates. SDS‐PAGE of metmyoglobin recovered from both fractions indicates gradual formation of covalently bound polymers upon storage. Isoelectric focusing (IEF) shows formation of new bands and zones with a drastic acidic shift of isoelectric points. Two‐dimensional IEF/SDS‐PAGE shows that the newly formed bands on IEF correspond to covalently bound myoglobin polymers.
No takes yet. Share an insight, caveat, or question.
Nakhost et al. (1983) studied this question.
Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context: