IDENTIFICATION OF DROSOPHILA THORAX PROTEINS AND THEIR DISTRIBUTION IN 2 TYPES OF MUSCLES

Protein composition of the Drosophila whole thorax was analyzed by two-dimensional polyacrylamide gel electrophoresis (2D-EP) and nonequilibrium pH gradient electrophoresis (NEpHGE). Altogether, approximately 300 protein spots in the thorax were detected reproducibly and 27 proteins had been identified their characteristics. To analyze the differential distribution of the protein spots in two types of muscles, fibrillar and tubular type muscle fibers were individually dissected from the thoraces of freeze-dried flies and were subjected separately to 2D-EP and NEpHGE. 66 protein spots and 14 protein spots were detected specifically in fibrillar muscles and tubular muscles, respectively. 24 protein spots were detected more abundantly in fibrillar muscles than in tubular muscles: 5 protein spots were detected more abundantly in tubular muscles than in fibrillar muscles. 4 proteins existed in both muscles similarly. This study would provide the useful basis for the molecular and genetical studies of Drosophila muscles.