| Autor: |
Daniel JM; Department of Chemistry, Swiss Federal Institute of Technology, ETH, CH-8093, Zürich, Switzerland., McCombie G, Wendt S, Zenobi R |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of the American Society for Mass Spectrometry [J Am Soc Mass Spectrom] 2003 May; Vol. 14 (5), pp. 442-8. |
| DOI: |
10.1016/S1044-0305(03)00132-6 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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