Abstract
A lipid peroxidation enzyme system of channel catfish (Ictalurus punctatus) muscle microsomes was identified and characterized. The enzyme system preferred NADH to NADPH as a cofactor to catalyze lipid oxidation. High levels of ADP and NADH, but not ferric ion, were inhibitory in the system. Ferrous ion had a greater promoting effect on lipid peroxidation than ferric ion in catfish muscle microsomes. ATP was more effective than ADP in activating the enzyme system, but AMP had little effect on activating lipid oxidation. The optimal temperature for activity was 30°C and the optimal pH was around 6.9. MnCl2 , p-hydroxymercuribenzoate (pHMB), KCN, and sodium benzoate had a complete inhibitory effect on the lipid peroxidation enzyme system.
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