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Klassische Synthese eines selektiven Peptid-Substrates für die Messung der Proteinkinase C

✍ Scribed by Spencker, Torsten ;Goppelt-Struebe, Margarete ;Keese, Wolfgang ;Resch, Klaus ;Rimpler, Manfred

Publisher: John Wiley and Sons
Year: 1993
Tongue: English
Weight: 446 KB
Volume: 1993
Category: Article
ISSN: 0947-3440
DOI: 10.1002/jlac.199319930142

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✦ Synopsis

Conventional Synthesis of a Selective Peptide Substrate for Measurements of Protein Kinase C

Protein kinase C (PKC), a family of serin/threonin kinases, plays a key role in signal transduction. We have prepared the PKC‐selective peptide substrate H‐Phe‐Lys‐Lys‐Ser‐Phe‐Lys‐Leu‐NH~2~ (7) by classical solution synthesis. 7 allows PKC‐measurements in crude extracts or permeabilized cells. The protection of the N‐terminal amino acid and the side chains by Boc resp. tert‐butyl groups enables a one‐step liberation of the desired heptapeptide amide 7.

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