Mapping of Tyrosine Kinase Autophosphorylation Sites with Synthetic Peptide Substrates. Streamlined peptide chemical approach to delineate possible tyrosine phosphorylation sites in a protein kinase. Once identified, these tyrosine phosphopeptides facilitate in vitro and in vivo site determination. Analytical Biochemistry 216, 135-146. An Improved Procedure for Enzymatic Digestion of Polyvinylidene Difluoride-Bound Proteins for Internal Sequence Analysis.
Pmol sensitivity is demonstrated.
Thorough practical account by a leading laboratory in this field on the optimization of HPLC components, sample manipulation, and downstream analysis of synthetic or proteolytically derived peptides at pmol levels. Analytical Biochemistry 223, 74-81. Evaluation of Two-Dimensional Phosphopeptide Maps by Electrospray Ionization Mass Spectrometry of Recovered Peptides. A chromatographic procedure to enrich samples is also given. Analytical Biochemistry 221, 374-378.