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- W125014789 abstract "Publisher Summary This chapter presents a study involving the identification of phosphorylation sites in large membrane proteins following their isolation by SDS-PAGE. Rat brain sodium channels were partially purified through the step of wheat germ agglutinin chromatography. A preparation containing 1200 pmol sodium channels was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase in the presence of 0.5 mM [γ-32P]ATP for 30 min at 37°C. The reaction was stopped by the addition of SDS-PAGE sample buffer and incubation at 55°C for 15 min. Rabbit skeletal muscle L-type calcium channels were purified, and a preparation containing 500 pmol was phosphorylated for the sodium channel. The primary structure of the rat brain type II sodium channel α subunit predicts six potential cAMP-dependent phosphorylation sites between residues 554 and 687." @default.
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- W125014789 date "1993-01-01" @default.
- W125014789 modified "2023-10-16" @default.
- W125014789 title "The Identification of Phosphorylation Sites in Large Membrane Proteins Following Their Isolation by SDS-PAGE" @default.
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- W125014789 doi "https://doi.org/10.1016/b978-0-12-058757-5.50025-1" @default.
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