Group fractionation and determination of the number of ribosomal subunit proteins from Drosophila melanogaster embryos.
Proteins were extracted from ribosomes and (for the first time) from ribosomal subunits of Drosophila melanogaster embryos. The ribosomal proteins were analyzed by two-dimensional polyacrylamide gel electrophoresis. The electrophoretograms displayed 78 spots for the 80S monomers, 35 spots for the 60S subunits, and 31 spots for the 40S subunits. On the basis of present information, we propose what we believe to be a reliable and convenient nomenclature for the proteins of the ribosomes and each of the subunits. A pair of acidic proteins from D. melanogaster appears to be very similar in electrophoretic mobility to the acidic proteins L7/L12 from Escherichia coli and L40/L41 from rat liver. The electrophoretogram of proteins from embryonic ribosomes shows both qualitative and quantitative differences from those of larvae, pupae, and adults previously reported by others. The proteins of the 40S subunit range in molecular weight from approximately 10,000 to 50,000, and those from the 60S subunit range from approximately 11,000 to 50,000.
D000818:Animals; D005591:Chemical Fractionation; D002850:Chromatography, Gel; D004331:Drosophila melanogaster / Q000032:analysis* / Q000196:embryology; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D009626:Terminology as Topic
D012269:Ribosomal Proteins