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Klassische Synthese eines selektiven Peptid‐Substrates für die Messung der Proteinkinase C
Author(s) -
Spencker Torsten,
GoppeltStruebe Margarete,
Keese Wolfgang,
Resch Klaus,
Rimpler Manfred
Publication year - 1993
Publication title -
liebigs annalen der chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0170-2041
DOI - 10.1002/jlac.199319930142
Subject(s) - chemistry , protein kinase c , substrate (aquarium) , stereochemistry , kinase , peptide , biochemistry , oceanography , geology
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 .