Use of peptide substrates for affinity purification of protein-serine kinases.

Abstract

The ability of protein kinases to phosphorylate synthetic peptides corresponding to identified protein phosphorylation sites has previously been used to determine primary structural requirements and has helped define distinct "recognition sequences" for a variety of enzymes. Here, we have used an immobilized synthetic peptide derived from glycogen synthase… (More)

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Cite this paper

@article{Woodgett1989UseOP, title={Use of peptide substrates for affinity purification of protein-serine kinases.}, author={James R Woodgett}, journal={Analytical biochemistry}, year={1989}, volume={180 2}, pages={237-41} }