Modification of ribosomal proteins in sea urchin eggs following fertilization

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Abstract
Analysis of the ribosomal proteins in sea urchin eggs by 2-dimensional polyacrylamide gel electrophoresis revealed postfertilization changes in the proteins of the small and the large subunits. Five egg-ribosomal proteins (S7, S16, S19, L19, L31) appeared to undergo rapid changes to the corresponding embryo-specific proteins. These changes were completed within 30 min after fertilization; identical electrophoretic patterns were observed among the different developmental stages of embryos. Of the 5 proteins, S7 showed an increase in the phosphorylated form. The remainder showed qualitative shifts to the corresponding embryo-specific proteins; peptide map analyses revealed the existence of common structural units between the corresponding proteins. These modifications were observed in the 3 spp. of sea urchin studied (Pseudocentrotus depressus, Hemicentrotus pulcherrimus and Anthocidaris crassispina), except in the case of 1 protein (L31). Purification of ribosomes by different procedures based on high-salt treatment gave the same results with respect to the egg-specific and embryo-specific proteins.