Abstract
Determination of phosphorylation sites in proteins is usually accomplished using [γ-32P]ATP. For low-abundance phosphoproteins,in vivoand intact cell studies usually require millicurie levels of32P for a single experiment, making multiple experiments prohibitive. Here we describe a low picomole sensitivity, nonradioisotopic, high-throughput method for tracing phosphorylation sites in proteins and peptides. The method is based onin situenzyme-linked immunosorbent assay (ELISA) plate biotinylation of nonphospho- and phosphopeptides, streptavidin capture, and ELISA detection using recently available anti-phospho-Thr and anti-phospho-Ser antibodies.
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