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

Citation
Mj. Benitez et al., Binding of polylysine to protein kinase CK2, measured by surface plasmon resonance, MOL C BIOCH, 191(1-2), 1999, pp. 29-33
Citations number
27
Categorie Soggetti
Cell & Developmental Biology
Journal title
MOLECULAR AND CELLULAR BIOCHEMISTRY
ISSN journal
03008177 → ACNP
Volume
191
Issue
1-2
Year of publication
1999
Pages
29 - 33
Database
ISI
SICI code
0300-8177(199901)191:1-2<29:BOPTPK>2.0.ZU;2-L
Abstract
The interaction between protein kinase CK2 and polylysine has been studied by Surface Plasmon Resonance (SPR). The binding process has a very low ener gy of activation, it is irreversible, and too slow as to explain the enzyme activity stimulation as a direct consequence of the polylysine binding. Th e polylysine interaction with a peptide substrate and with casein are faste r, and in agreement with a substrate-mediated mechanism of activity stimula tion. After several hours of incubation, the binding of polylysine to CK2 p roduces the loss of enzymatic activity.