CONVENTIONAL SYNTHESIS OF A SELECTIVE PEPTIDE SUBSTRATE FOR MEASUREMENTS OF PROTEIN-KINASE-C

被引：0
|
作者：
SPENCKER, T
GOPPELTSTRUEBE, M
KEESE, W
RESCH, K
RIMPLER, M
机构：
[1] HANNOVER MED SCH, INST MED CHEM, KONSTANTY GUTSCHOW STR 8, W-3000 HANNOVER 61, GERMANY
[2] HANNOVER MED SCH, INST MOLEK PHARMAKOL, W-3000 HANNOVER 61, GERMANY
来源：
LIEBIGS ANNALEN DER CHEMIE | 1993年 / 03期
关键词：
PROTEINKINASE-C; MARCKS-PROTEIN; ENZYMES; AMINO ACIDS; PEPTIDES;
D O I：
暂无
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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, (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.
引用
收藏
页码：237 / 240
页数：4
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