Abstract
Progress in clinicopathological research for hemoglobinopathies and neurodegenerative diseases have increased the need for simple and definite methods to detect and characterize mutant proteins, e. g., amyloid protein, Cu/Znbinding superoxide dismutase (SOD-1), prion protein accociated with the diseases. The DNA analysis is a simpler current method for detection of mutations, however, it does not elucidate the post-genome informations such as the posttranslational modification, protein-protein or -DNA interactions and the ratio of wild to mutant proteins, which are not available directly from the genome. The mass spectrometry (MS) may offer a powerful tool for these postgenome analysis. In 1994, we have established immunoprecipitation as a simple and reliable procedure for detecting mutant protein by MALDI-TOFMS and by HPLC-ESIMS. By this procedure, the isolation, concentration and desalting of the mutant proteins to be tested could be achieved simultaneously. Herein, we applied this technique for the detection of mutant proteins associated with diseases such as familial amyotrophic lateral sclerosis, familial amyloid polyneuropathy, hemoglobinopathies and characterized some mutant proteins included new mutations by MS.
