Rgr. Chou et al., POSTMORTEM CHANGES IN MYOFIBRILLAR PROTEINS OF BREAST AND LEG MUSCLESFROM BROILERS, SPENT HENS AND TAIWANESE COUNTRY CHICKENS, Journal of the Science of Food and Agriculture, 65(3), 1994, pp. 297-302
Post mortem ageing at 4 degrees C was studied in the breast and leg mu
scles from broilers, White Leghorn spent hens and Taiwanese Country Ch
ickens (TCC). Purified myofibrils were prepared from muscles after 0,
1, 3, 5, and 7 days of post mortem storage at 4 degrees C. SDS-PAGE wa
s used to examine the changes in myofibrillar proteins of the muscles.
Results showed that 30 kDa components appeared earlier in the breast
muscles than in the leg muscles and in the order: broiler, TCC, and sp
ent hen. The intensity of 30 kDa band increased with post mortem time.
In the breast muscles, a decrease in the intensity of the alpha-actin
in band could be observed at 1 day post mortem in broilers and TCC and
at 3 days post mortem in spent hens. This decrease, however, could no
t be found in the leg samples until 5 or 7 day post mortem. Titin 1 ba
nd disappeared within 3 day post mortem in the breast samples but with
in 5 days in the leg samples. Similar results could be observed in the
degradation of nebulin although traces of nebulin remained in the leg
muscles of TCC after 7 days post mortem