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- W2002021027 abstract "A synthetic peptide Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala, the structure of which is based on that of a phosphorylated sequence in ribosomal protein S6, was employed as a probe for stimulated kinase activity in Xenopus laevis oocytes induced to mature with insulin or progesterone. Insulin elicited an early (20-30 min) 3-fold stimulation of S6 peptide phosphorylating activity that was not evident with progesterone. However, both hormones produced a delayed 7-12-fold stimulation of S6 peptide phosphorylating activity at the time of germinal vesicle breakdown. The results of DEAE-Sephacel, Sephacryl S-200, TSK-400, and heparin-Sepharose chromatographic fractionation experiments imply that a common S6 peptide kinase is activated as a consequence of short and long term insulin exposure, as well as in long term progesterone treatment of oocytes. Omission of potassium from the oocyte culture medium greatly facilitated insulin-induced meiotic maturation." @default.
- W2002021027 created "2016-06-24" @default.
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- W2002021027 date "1988-12-05" @default.
- W2002021027 modified "2023-10-16" @default.
- W2002021027 title "Insulin and progesterone activate a common synthetic ribosomal protein S6 peptide kinase in<i>Xenopus</i>oocytes" @default.
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- W2002021027 doi "https://doi.org/10.1016/0014-5793(88)81060-3" @default.
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