Purification of Drosophila acidic ribosomal proteins.

The relatively acidic proteins (group A80) of Drosophila melanogaster ribosomes were separated by ion-exchange chromatography. Fractions containing one or more acidic proteins were combined into thirteen pools. The criterion for the combination was the migration pattern in one-dimensional polyacrylamide gels containing sodium dodecyl sulphate. Five proteins (7/8, S25/S27, S14, L1/L2 and L5/L6) required no further purification. The others were further purified as follows: proteins S7, and S9 by preparative gel electrophoresis: and protein 13 (to newly identified protein) by adsorption with conconavalin-A--agarose. Four proteins had no detectable contamination, and in each of the others the impurities were no greater than 3%. The amount of purified protein recovered from a starting amount of 2.63 g total 80-S ribosomal protein and a starting amount of 105 mg group A80 varied from 0.4 mg to 8.8 mg. The molecular weight of the proteins was estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulphate. The amino acid composition of the individual purified proteins was determined. Several phosphorylated proteins were identified. Proteins 13b and 13c are phosphorylated derivatives of 13a; 7b/8b and 7c/8c are phosphorylated derivatives of 7a and/or 8a. Proteins 7/8 and 13 are distinct proteins but are very similar in amino acid composition.