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Fast‐atom bombardment tandem mass spectrometry of cyclic nucleotide analogues used as site‐selective activators of cyclic nucleotide‐dependent protein kinases
Author(s) -
Walton Terence J.,
Bayliss Mark A.,
Pereira M. Luisa,
Games David E.,
Genieser H.G.,
Brenton A. Gareth,
Harris Frank M.,
Newton Russell P.
Publication year - 1998
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19980430)12:8<449::aid-rcm174>3.0.co;2-v
Subject(s) - chemistry , nucleotide , cyclic nucleotide , gene isoform , fast atom bombardment , mass spectrometry , protein kinase a , kinase , stereochemistry , enzyme , adenosine , biochemistry , chromatography , gene
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, N 6 ‐ethenoadenosine‐3′,5′‐cyclic monophosphate (ϵ‐cyclic AMP) and 2′‐aza‐1, N 6 ‐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, N 6 ‐ 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.