Abstract
A synthetic peptide (APRTPGGRC) cross-linked to poly-L-lysine through a carboxy-terminal cysteinyl residue was found to be a highly specific substrate for mitogen-activated protein (MAP) kinases. This peptide conjugate exhibited a much lower Km value (74 microM) than the free peptide substrate (APRTPGGRR, Km > 1 mM) previously used as a specific substrate for MAP kinases. Unlike myelin basic protein, which has been often used as a substrate for MAP kinases, this conjugate did not serve as substrate for cAMP-dependent protein kinase, protein kinase C, or multifunctional calmodulin-dependent protein kinases. Using the peptide conjugate as a substrate, MAP kinase activities in crude cell extracts were directly determined by in vitro assay and specifically detected by in-gel assay.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
