SDS-Polyacrylamide Electrophoresis Pattern Alteration of Myofibrillar Proteins after Heating of Avian Leg and Breast Muscle

Abstract

The SDS-polyacrylamide disc gel electrophoresis patterns of myofibrillar proteins from leg and breast avian muscle heated to 45, 50, 55, and 60 C were evaluated. Most of the detected bands were tentatively identified on the basis of molecular weight calculated from their Rm (relative mobility). Heating the tissue caused denaturation of protein which resulted in reduced intensity and ultimate disappearance of the bands as temperature increased. Bands identified as myosin were quite sensitive to heat compared to the greater resistance of the G-actin band.