Abstract
Loss of solubility of sarcoplasmic proteins was used as an index for denaturation of leg and breast chicken muscle tissue water extracts heated to 40, 50, 60, 70, and 80 C. Proteins of the dark and light tissue proved to be different in heat sensitivity and electrophoresis patterns. After electrophoretic separation, some sarcoplasmic proteins from both leg and breast tissue yielded similar Rm (relative mobility) values but had different heat sensitivities. An electrophoresis band with the thermoinactivation characteristics of myoglobin was detected in the dark muscle tissue but not in light muscle.
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