NDLI: Isomeric discrimination and quantification of thyroid hormones, T$_{3}$ and rT$_{3}$, by the single ratio kinetic method using electrospray ionization mass spectrometry

Content Provider	Springer Nature Link
Author	Kumar, Avvaru Praveen Jin, Hua Jo, Sung Chan Kim, Changdae Nam, Sang Ho Lee, Yong Ill
Copyright Year	2010
Abstract	The single ratio kinetic method is applied to the discrimination and quantification of the thyroid hormone isomers, 3,5,3′-triiodothyronine and 3,3′,5′-triiodothyronine, in the gas phase, based on the kinetics of the competitive unimolecular dissociations of singly charged transition-metal ion-bound trimeric complexes [M$^{II}$(A)(ref)$_{2}$-H]$^{+}$ (M$^{II}$ = divalent transition-metal ion; A=T$_{3}$ or rT$_{3}$; ref = reference ligand). The trimeric complex ions are generated using electrospray ionization mass spectrometry and the ions undergo collisional activation to realize isomeric discrimination from the branching ratio of the two fragment pathways that form the dimeric complexes [M$^{II}$(A)(ref)-H]$^{+}$ and [M$^{II}$(ref)$_{2}$-H]$^{+}$. The ratio of the individual branching ratios for the two isomers R$_{iso}$ is found strongly dependent on the references and the metal ions. Various sets are tried by choosing the reference from amino acids, substituted amino acids, and dipeptides in combination with the central metal ion chosen from five transition-metal ions (Co$^{II}$, Cu$^{II}$, Mn$^{II}$, Ni$^{II}$, and Zn$^{II}$) for the complexes in this experiment. The results are compared in terms of the isomeric discrimination for the T$_{3}$/rT$_{3}$ pair. Calibration curves are constructed by relating the ratio of the branching ratios against the isomeric composition of their mixture to allow rapid quantitative isomer analysis of the sample pair. Furthermore, the instrument-dependence of this method is investigated by comparing the two sets of results, one obtained from a quadrupole ion trap mass spectrometer and the other from a quadrupole time-of-flight mass spectrometer.
Starting Page	14
Ending Page	22
Page Count	9
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	21
Issue Number	1
e-ISSN	18791123
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-11-22
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Analytical Chemistry Biotechnology Organic Chemistry Proteomics Bioinformatics
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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