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- W1968707041 abstract "The interaction between phosducin and βγ-transducin plays regulatory roles in light adaptation of photoreceptors. Both phosducin and βγ-transducin undergo post-translational modifications, with phosducin modified by phosphorylation and the γ subunit of βγ-transducin by farnesylation and carboxylmethylation. In this study we exploited the electrophoretic mobilities of these native proteins to develop a micro binding assay and examined the effects of post-translational modifications on binding affinities. It was found that decarboxylmethylation of γ-transducin increased the mobility of βγ-transducin during native gel electrophoresis, but decreased the apparent affinity for phosducin by about 2-fold. Phosphorylation of phosducin by protein kinase A increased the mobility but decreased the apparent affinity for βγ-transducin by at least 3-fold." @default.
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- W1968707041 date "1997-04-01" @default.
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- W1968707041 title "Phosducin and βγ-Transducin Interaction I: Effects of Post-translational Modifications" @default.
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- W1968707041 doi "https://doi.org/10.1006/bbrc.1997.6460" @default.
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