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Synthesis and binding studies of the 116-mer peptide containing the double cysteine-rich motifs of protein kinase C gamma

The 116-mer peptide containing the double cysteine-rich motifs of mouse protein kinase Cγ (γ-C1A-C1B) has been synthesized using an Fmoc-solid phase strategy with a stepwise chain elongation. The peptide was purified only by reversed phase HPLC and gave satisfactory mass data (MALDI-TOF-MS and ESI-T...

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Bibliographic Details
Published in:Tetrahedron letters 1998-10, Vol.39 (43), p.7943-7946
Main Authors: Fukuda, Hiroyuki, Irie, Kazuhiro, Nakahara, Akifumi, Oie, Kentaro, Ohigashi, Hajime, Wender, Paul A
Format: Article
Language:English
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Summary:The 116-mer peptide containing the double cysteine-rich motifs of mouse protein kinase Cγ (γ-C1A-C1B) has been synthesized using an Fmoc-solid phase strategy with a stepwise chain elongation. The peptide was purified only by reversed phase HPLC and gave satisfactory mass data (MALDI-TOF-MS and ESI-TOF-MS). Scatchard analysis of the zinc-folded peptide revealed two binding sites of distinct affinities ( K d = 6.0 and 47.0 nM) comparable to those reported by Quest and Bell for GST-γ-C1A-C1B fusion protein prepared by DNA recombination.
ISSN:0040-4039
1873-3581
DOI:10.1016/S0040-4039(98)01768-7