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Daniel, J.M.* ; McCombie, G.* ; Wendt, S.* ; Zenobi, R.*

Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors.

J. Am. Soc. Mass Spectrom. 14, 442-448 (2003)
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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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
e-ISSN 1044-0305
Zeitschrift Journal of the American Society for Mass Spectrometry
Quellenangaben Band: 14, Heft: 5, Seiten: 442-448 Artikelnummer: , Supplement: ,
Verlag Elsevier
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Toxicology and Pharmacology (TOX)