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Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA
Reprint requests to: J. Throck Watson, Michigan State University, 401 Biochemistry Bldg., MSU Campus, East Lansing, MI 48824, USA; e-mail: watsonj{at}msu.edu.; fax: (517) 353-9334.
Under specified UV-MALDI conditions, the 4-dimethylaminophenylazophenyl-4-maleimide (DABMI) derivative of cysteine-containing peptides undergoes prompt fragmentation to produce a characteristic mass spectral pattern. As reported previously by others, derivatization with chromophoric DABMI allows cysteine-containing peptides and proteins to be tracked during HPLC by absorbance at upper UV and visible wavelengths. Here, we describe methodology by which these same peptide derivatives can be recognized by their distinctive MALDI mass spectral fragmentation pattern, then mass mapped, allowing for easy, rapid identification of cysteine-containing peptides.
Keywords: DABMI; prompt fragmentation; MALDI
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