Proteomic profiling of large myofibrillar proteins from dried and long-term stored polyacrylamide gels.

A method for the utilization of dried polyacrylamide gels from the pre-proteomic era is described in order to enable the mass spectrometric analysis of long-term stored protein preparations. The in-gel digestion of high-molecular-mass proteins embedded in a 20-year old gel was carried out following gel re-swelling and resulted in the proteomic identification of a large number of proteins, including 3400 kDa titin, 800 kDa nebulin and myosin heavy chains of 220 kDa from rabbit skeletal muscle. These findings demonstrate that dried protein gels from past biochemical analyses can be successfully reused and analyzed by modern and refined mass spectrometric techniques.