DSpace

Digital.CSIC > Ciencia y Tecnologías Físicas > Instituto de Microelectrónica de Madrid (IMM-CNM) > (IMM-CNM) Artículos >

Share

EndNote

Impact

Links

Closed Access item Binding of polylysine to protein kinase CK2, measured by Surface Plasmon Resonance

Authors:Benítez, María J.
Mier, Gerardo
Briones Fernández-Pola, Fernando
Moreno, Francisco J.
Jiménez, Juan S.
Keywords:Polylysine, CK2, Surface Plasmon Research
Issue Date:1999
Publisher:Springer
Citation:Molecular and Cellular Biochemistry 191 (1): 29-33 (1999)
Abstract: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.
Publisher version (URL):http://dx.doi.org/10.1023/A:1006821520346
URI:http://hdl.handle.net/10261/34946
ISSN:0300-8177
E-ISSNmetadata.dc.identifier.doi = DOI:1573-4919
???metadata.dc.identifier.doi???:10.1023/A:1006821520346
Appears in Collections:(IMM-CNM) Artículos

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.