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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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Published in: | Tetrahedron letters 1998-10, Vol.39 (43), p.7943-7946 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0040-4039 1873-3581 |
DOI: | 10.1016/S0040-4039(98)01768-7 |