Identification of calcium binding proteins in two-dimensional gel electrophoretic pattern of Drosophila thorax and their distribution in two types of muscles.
Ten Drosophila thorax proteins (six myosin light chains and four proteins called a, b, c, d) were found to have high affinities with Ca2+. This was proved after subjecting the total Drosophila thorax proteins to two-dimensional (2D) transblot, followed by 45Ca2+ autoradiography. Three proteins (a, c, d) showed Ca2+ dependent electrophoretic mobility changes. To know their tissue-specific localization, fibrillar and tubular type muscle fibers were individually dissected from freeze-dried flies and separately subjected to 2D gel electrophoresis. Fibrillar type muscle had protein b and a small amount of protein a. Tubular type muscle had proteins c, d and a very large amount of protein a. Protein d was characterized to be calmodulin.
Tanaka
Y
Y
Department of Physics, Faculty of Science, University of Tokyo.
Maruyama
K
K
Mikawa
T
T
Hotta
Y
Y
D000818:Animals; D001345:Autoradiography / Q000379:methods; D002135:Calcium-Binding Proteins / Q000032:analysis*; D002147:Calmodulin / Q000032:analysis; D004330:Drosophila; D015180:Electrophoresis, Gel, Two-Dimensional; D009132:Muscles / Q000032:analysis*; D013909:Thorax
D002135:Calcium-Binding Proteins; D002147:Calmodulin