Emerging bioanalysis applications for ICP-MS

The realization that elemental analysis offers signiflcant advantages to the field of protein quantitation has directed the development of several new methods of protein quantitation via inductively coupled plasma mass spectrometry (ICP-MS) linked immunoassays. This new technique provides an innovative arena for ICP-MS in the analysis of biological samples. 

Inductively Coupled Plasma Mass Spectrometry Handbook 

This section of the book details various methods and applications of measuring specific protein concentrations using the ICP-MS-linked metal-tagged immunoassays. 

Traditionally, antibodies have been tagged with radioisotopes, enzymes (e.g. horseradish peroxidase) or fluorochrome molecules. Thus the chemistry of antibody tagging has been well established and typically involves using accessible primary amines (e.g. lysines) and thiol groups (reduced cysteine disulfide bonds) for binding. The same methods are also used for coupling metal tags to antibodies. 

The advantages and disadvantages of each method were systematically analyzed. The protein targets examined included Smad proteins (which play a role in cardiac muscle development) and various regulatory proteins found in human serum which are involved in the immune response, including immunoglobin (IgG), interleukin-Ibeta (IL-IP), interleukin-6 (IL-6), interleukin-8 (IL-8), interleukin-13 (IL-13), interferon-gamma (lEN-y) and tumor necrosis factor-alpha (TNF-a). 

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