Differential scanning calorimetric studies of muscle and its constituent proteins

Abstract

Abstract Rabbit muscle and its constituent proteins were investigated by differential scanning calorimetry (d.s.c.). Post ‐ rigor muscle yielded a complex thermogram comprising at least three endothermic transitions with T max values of 60, 67 and 80°C. Comparison with the purified proteins or fractions indicated that these transitions corresponded to denaturation of myosin, sarcoplasmic proteins and actin respectively. In addition to these endothermic transitions, pre ‐ rigor muscle produced a single large exotherm of T max 54°C. The evidence suggested that this transition was closely linked with the process of contraction.