Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors.
J Am Soc Mass Spectrom
; 14(5): 442-8, 2003 May.
Article
en En
| MEDLINE
| ID: mdl-12745213
ABSTRACT
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.
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Bases de datos:
MEDLINE
Asunto principal:
Adenilato Quinasa
/
Espectrometría de Masa por Ionización de Electrospray
/
Inhibidores Enzimáticos
Tipo de estudio:
Risk_factors_studies
Límite:
Animals
Idioma:
En
Revista:
J Am Soc Mass Spectrom
Año:
2003
Tipo del documento:
Article
País de afiliación:
Suiza