Premium
Stable ion complexes of vitamin A species (retinol) in solution as detected by mass spectrometry
Author(s) -
SánchezGuijo Alberto,
Montero Olimpio
Publication year - 2010
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/rcm.4497
Subject(s) - chemistry , fragmentation (computing) , adduct , mass spectrometry , retinol , ion , vitamin , complex formation , medicinal chemistry , chromatography , stereochemistry , biochemistry , inorganic chemistry , organic chemistry , computer science , operating system
Mechanisms of retinol (ROL) transport in plasma alternative to that involving the Retinol‐Binding Protein (RBP) have been hypothesized after RBP‐knockout mice were shown to be viable and fertile. Accordingly, the possibility of a ROL fraction circulating free in plasma has been suggested. In this study, stable complex formation between ROL and the physiological relevant ions Na + , Li + , and K + was investigated by using mass spectrometry and assessed in regard to the aforementioned alternative mechanism. The ROL‐Na complex was found to be kinetically favoured with respect to the ROL‐Li and ROL‐K complexes. Fragmentation of the [ROL‐Na] + adduct rendered the carbocation [ROL+H–H 2 O] + ( m/z 269) and NaOH as neutral loss. In consonance with these results, it is hypothesized on the possibility of the complex [ROL‐Na] + being an alternative way of ROL transport to cells, as well as an intermediate in cis / trans isomerism. Copyright © 2010 John Wiley & Sons, Ltd.