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Matrix Effects on the Fragmentation of Vitamin B 12 in Plasma Desorption Mass Spectrometry
Author(s) -
Blankenship J. F.,
VanStipdonk M. J.,
Schweikert E. A.
Publication year - 1997
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(19970115)11:1<143::aid-rcm814>3.0.co;2-z
Subject(s) - chemistry , analyte , corrin , fragmentation (computing) , mass spectrometry , desorption , protonation , analytical chemistry (journal) , ion , yield (engineering) , matrix assisted laser desorption/ionization , matrix (chemical analysis) , chromatography , inorganic chemistry , organic chemistry , cobalt , adsorption , materials science , computer science , metallurgy , operating system
A continuing effort in mass spectrometry is to optimize desorption/ionization processes in order to enhance analyte ion yields and reduce fragmentation. The effect of small carbohydrate and amino acid matrices on the yield of secondary ions from vitamin B 12 (cyanocobalamin) was examined using plasma desorption mass spectrometry. The extent of the corrin decomposition is dependent upon the matrix‐to‐analyte ratio. The enhanced yields of the high‐mass fragment ion [M–CN + H] + and the ions corresponding to protonated molecules, however, are dependent upon both the matrix‐to‐analyte ratio and the nature of the matrix. © 1997 John Wiley & Sons, Ltd.