Home
Deutsch
Advanced Search
Browse by ...
Publication overview
Contact persons
Help
PMC
 |
|
Open Access Green as soon as Postprint is submitted to ZB.
Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors.
J. Am. Soc. Mass Spectrom. 14, 442-448 (2003)
Noncovalent complexes between chicken muscle adenylate kinase and two inhibitors, P(1),P(4)-di(adenosine-5')tetraphosphate (Ap4A) and P(1),P(5)-di(adenosine-5') pentaphosphate (Ap5A), were investigated with electrospray ionization mass spectrometry under non-denaturing conditions. The nonconvalent nature and the specificity of the complexes are demonstrated with a number of control experiments. Titration experiments allowed the association constants for inhibitor binding to be determined. Problems with concentration dependent ion yields are circumvented by a data evaluation method that is insensitive to the overall ionization efficiency. The K(a) values found were 9.0 x 10(4) M(-1) (Ap4A) and 4.0 x 10(7) M(-1) (Ap5A), respectively, in very good agreement with available literature data.
Altmetric
Additional Metrics?
Edit extra informations
Login
Publication type
Article: Journal article
Document type
Scientific Article
e-ISSN
1044-0305
Quellenangaben
Volume: 14,
Issue: 5,
Pages: 442-448
Publisher
Elsevier
Reviewing status
Peer reviewed