Binding of polylysine to protein kinase CK2, measured by surface plasmon resonance

被引：6

作者：

Benitez, MJ

Mier, G

Brione, F

Moreno, FJ

Jiménez, JS

机构：

[1] Univ Autonoma Madrid, Dept Quim Fis Aplicada, E-28049 Madrid, Spain

[2] CSIC, Ctr Nacl Microelect, E-28006 Madrid, Spain

[3] Univ Autonoma Madrid, Ctr Biol Mol Severo Ochoa, CSIC, Madrid, Spain

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1999年 / 191卷 / 1-2期

关键词：

CK2; polylysine; Surface Plasmon Resonance;

D O I：

10.1023/A:1006821520346

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The interaction between protein kinase CK2 and polylysine has been studied by Surface Plasmon Resonance (SPR). The binding process has a very low energy of activation, it is irreversible, and too slow as to explain the enzyme activity stimulation as a direct consequence of the polylysine binding. The polylysine interaction with a peptide substrate and with casein are faster, and in agreement with a substrate-mediated mechanism of activity stimulation. After several hours of incubation, the binding of polylysine to CK2 produces the loss of enzymatic activity.

引用

页码：29 / 33

页数：5

共 27 条

[11]

HATHAWAY GM, 1979, J BIOL CHEM, V254, P762

[12]

HATHAWAY GM, 1982, CURR TOP CELL REGUL, V21, P101

[13] CASEIN KINASES - PLEIOTROPIC MEDIATORS OF CELLULAR-REGULATION [J].