A colorimetric enzyme‐linked on‐bead assay for identification of synthetic substrates of protein tyrosine kinases
- 9 April 2002
- journal article
- research article
- Published by Wiley in Journal of Peptide Science
- Vol. 8 (5) , 227-233
- https://doi.org/10.1002/psc.376
Abstract
Protein tyrosine kinases play key roles in the progression of numerous human diseases including several types of cancers. We report here a simple colorimetric assay for tyrosine kinase activity employing synthetic peptide substrates prepared on Tentagel synthesis beads. Phosphorylation of compounds on beads was detected with an antiphosphotyrosine antibody complexed with a secondary antibody–alkaline phosphatase conjugate. This assay may prove useful for the identification and characterization of synthetic substrates of this important class of enzymes. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.Keywords
This publication has 29 references indexed in Scilit:
- Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine KinaseScience, 2000
- Protein Tyrosine Kinase Structure and FunctionAnnual Review of Biochemistry, 2000
- Bivalent Inhibitors of Protein Tyrosine KinasesJournal of the American Chemical Society, 1998
- Synthesis and Screening of Linear and Cyclic Oligocarbamate Libraries. Discovery of High Affinity Ligands for GPIIb/IIIaJournal of the American Chemical Society, 1998
- Application of “one-bead one-compound” combinatorial library methods in signal transduction researchLife Sciences, 1998
- The “One-Bead-One-Compound” Combinatorial Library MethodChemical Reviews, 1997
- Identification and characterization of a novel synthetic peptide substrate specific for Src‐family protein tyrosine kinasesInternational Journal of Peptide and Protein Research, 1995
- Catalytic specificity of protein-tyrosine kinases is critical for selective signallingNature, 1995
- Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signalingCell, 1995
- Identifying Substrate Motifs of Protein Kinases by a Random Library ApproachBiochemistry, 1994