To investigate the physico-chemical characteristics, myofibrils and actomyosins were prepared from white and red muscle of day-old chick, broiler and cull layer. The results were summarized as follows. 1. In the case of day-old chick, the SDS-polyacry...
To investigate the physico-chemical characteristics, myofibrils and actomyosins were prepared from white and red muscle of day-old chick, broiler and cull layer. The results were summarized as follows. 1. In the case of day-old chick, the SDS-polyacrylamide gel electrophoretograms of myofibril from red muscle were different from that of white muscle, while those of broiler and cull layer were same. 2. The Ca-activated ATPase activity of actomyosin increased in the order of cull layer, broiler and day-old chick. The enzymatic activity was higher in the white muscle compared to red muscle in all three age groups, regardless of KCI concentration and pH. However, in the case of day-old chick, KCI concentration dependency of Ca-activated ATPase activity was not observed. 3. The Mg-activated ATPase activity of actomyosin was higher at 0.02M KCI concentration, and decreased remarkably as the ionic strength increased in all muscle fiber types and age groups. 4. The effect of KCI concentration on the solubility of actomyosin was different. The solubility of actomyosin from day-old chick, broiler and cull layer increased remarkably at 0.25 M, 0.4 M and 0.55 M KCI concentration, respectively. 5. The thermostability of actomyosin decreased as the heating temperature increased. The thermostability of actomyosin from white muscle was higher than that of red muscle and actomyosins from day-old chick muscles were more heatlabile than those from broiler and cull layer.