Abstract
Reduced trout haemoglobin (Hb) is a mixture of oxy- and deoxy-Hb at pH 6.3. Addition of oxy/deoxyHb to washed muscle resulted in detectable ferryl Hb while adding bovine oxyHb, trout metHb, or bovine metHb did not. Trout metHb promoted lipid oxidation more rapidly than bovine metHb, attributable to lower haemin affinity in fish Hbs. Protoporphyrin IX degradation was prevalent during trout and bovine Hb-mediated lipid oxidation. Caffeic acid prevented porphyrin degradation and lipid oxidation. Crosslinked myoglobin (Mb) promoted lipid oxidation more effectively than metMb. Fish metMb released haemin more readily than mammalian metMb at pH 5.5. These studies suggest haemin dissociation from metHb causes formation of free radicals that degrade protoporphyrin and cause lipid oxidation, and appreciable quantities of deoxyHb are needed to generate ferryl Hb oxidant. Crosslinking appears to facilitate Mb-mediated lipid oxidation in washed muscle yet haemin release can occur from fish metMb at low pH.
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