A soluble calcium-binding protein (SCBP) present in Drosophila melanogaster and Calliphora erythrocephala muscle cells.
1. Soluble calcium binding proteins (SCBP) were isolated from homogenates of whole flies, from the thorax and from muscles of Drosophila melanogaster and Calliphora erythrocephala. 2. Crude preparations were obtained by extraction at low ionic strength, acid and heat treatment. The Drosophila protein was purified by gel filtration, hydrophobic interaction and ion exchange chromatography. In contrast to calmodulin the Drosophila SCBP did not bind to phenyl-Sepharose in a Ca(2+)-dependent way. 3. Both the Drosophila and the Calliphora protein revealed identical properties. 4. The apparent molecular mass of the SCBP is 24 kDa. Separation in urea-PAGE demonstrated the existence of two isoforms. 5. The calcium-binding property was assured by a calcium dependent electrophoretic mobility shift and autoradiography of 45Ca(2+)-incubated Western blots. 6. The proteins are abundant in the thorax and were even detectable in crude extracts of various muscles (leg muscles and the extracoxal depressor). In contrast, in power muscles and in the thoracic ganglion the proteins could not be observed.
Kiehl
E
E
Institut für Zoologie, Universität Düsseldorf, Germany.
D'Haese
J
J
D000818:Animals; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004175:Diptera / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification / Q000378:metabolism; D012995:Solubility; D013045:Species Specificity
D002135:Calcium-Binding Proteins; D009124:Muscle Proteins