Ribosomal protein S6 from Xenopus laevis ovaries was prepared by ion-exchange chromatography on phosphocellulose and gel filtration on Sephadex G-75. The protein was identified as S6 from its position on two-dimensional polyacrylamide gels and from its immunological cross-reaction with monoclonal antibody raised against chicken liver S6, and from the fact that it is the major phosphorylated protein of the small subunit. When oocytes were incubated with [32P]orthophosphate in the presence of progesterone, 32P incorporation of 40-S ribosomal proteins was stimulated about 10-fold over controls without hormone. The bulk of the 32P radioactivity was incorporated into protein S6.
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Kalthoff et al. (1982) studied this question.
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