Fast-atom bombardment tandem mass spectrometry of cyclic nucleotide analogues used as site-selective activators of cyclic nucleotide-dependent protein kinases

Autor: Frank M. Harris, Russell P. Newton, H.-G. Genieser, Terence J. Walton, David E. Games, A. Gareth Brenton, M. Luisa Pereira, Mark A. Bayliss
Rok vydání: 1998
Předmět:
Zdroj: Rapid Communications in Mass Spectrometry. 12:449-455
ISSN: 1097-0231
0951-4198
Popis: The mass spectrometric behaviour of six cyclic nucleotide analogues which activate cyclic AMP-dependent protein kinase was studied by positive-ion fast-atom bombardment (FAB) and collision-induced dissociation (CID) mass-analysed ion kinetic energy (MIKE) spectrometry. The compounds studied were 1,N6-ethenoadenosine-3′,5′-cyclic monophosphate (ϵ-cyclic AMP) and 2′-aza-1,N6-ethenoadenosine-3′,5′- cyclic monophosphate, which each activate both isoforms of cyclic AMP-dependent protein kinase and have similar affinity for both the ‘fast’ and the ‘slow’ regulatory site of each isoform, N6 - phenyl-cyclic AMP, which is selective for the ‘fast’ regulatory site of each isoform, and 6-chloropurine riboside-3′,5′-cyclic monophosphate, 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole-3′,5′-cyclic monophosphate and 8-(4-chlorophenylthio)-adenosine-3′,5′-cyclic monophosphate, which are each selective for the ‘slow’ regulatory site and preferentially activate isoform II. The FAB- and CID/MIKE spectra of the analogues are discussed in relation to their use in studies of the regulation of protein kinase activity by quantitative FAB mass spectrometry. © 1998 John Wiley & Sons, Ltd.
Databáze: OpenAIRE
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