Identification of restricting factors that inhibit swelling of oxidized myofibrils during brine irrigation

Porcine longissimus myofibrils were exposed to a hydroxyl radical-oxidizing system (10 μM FeCl₃, 100 μM ascorbic acid, 1 mM H ₂O₂) at pH 6.2 for 1-12 h. Chemical analyses (sulfhydryls, disulfide bonds, carbonyls) indicated mild protein oxidation along with almost 40% loss of protein extractability in low-ionic-strength brines (≤0.4 M NaCI, 10 mM pyrophosphate, pH 6.2). Upon graded brine irrigation (0.2→0.6 M NaCl) with pyrophosphate, the swelling of myofibrils and the dissolution of the A-band of oxidized myofibrils were less pronounced than those of nonoxidized. This restriction of myofibril swelling, caused largely by disulfide cross-linkages formed between oxidized myosin tails, was positioned on the transversely expansible thick filaments, reflecting a significant role and susceptibility of intra- as well as intermyofilamental structures.