Identification of 30-kDa fat body protein of Sarcophaga peregrina larvae selectively phosphorylated in the presence of 20-hydroxyecdysone as ribosomal protein S6.
Previously, we showed that 20-hydroxyecdysone induces selective phosphorylation of a fat body protein of Sarcophaga peregrina with a molecular mass of about 30,000 (30-kDa protein) (Itoh, K., Ueno, K., & Natori, S. (1985) Biochem. J. 227, 683-688). This paper describes the identification of this 30-kDa protein. From the electrophoretic profile of 40S ribosomal proteins on two-dimensional polyacrylamide gel electrophoresis, the 30-kDa protein was identified as S6.
D000273:Adipose Tissue / Q000032:analysis*; D000818:Animals; D004175:Diptera; D004441:Ecdysterone / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005216:Fat Body / Q000032:analysis*; D007814:Larva / Q000032:analysis; D008970:Molecular Weight; D010766:Phosphorylation; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins / Q000378:metabolism*
D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins; D004441:Ecdysterone