PubMed · 14263268
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R B MERRIFIELD. 1965. SOLID-PHASE PEPTIDE SYNTHESES.. https://doi.org/10.1016/0160-9327(65)90090-6
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In the present paper, the covalent immobilisation of the digesting enzyme trypsin has been achieved through photo-immobilisation on a portion of a silica capillary, thus leading to the construction of a capillary electrophoretic (CE)-microreactor for peptide mapping. The CE-microreactor is characterised by being a single piece, thus ensuring no fluidic or electrical leakage. The enzyme was immobilised with a surface density of 15.8 microg/cm(2), the stability was high (80% after 38 days) and the rate of conversion was 0.2 ng/s. On-line protein mapping was tested with proteins of different dimensions, showing competitiveness in terms of time (completed map within 15 min) and exhaustive maps of small proteins. The results of the CE-microreactor and the potential to immobilise biocomponents easily on a desired portion of the capillary indicate further developments towards the construction of a variety of miniaturised enzymatic screening devices for high-throughput screening analysis.
A new ion mobility instrument that incorporates a low-field region for ion separation and a high-field region for collisional activation is described. In this approach, mixtures of ions are separated based on differences in their mobilities in a approximately 20-cm-long low-field ( approximately 5 V cm(-)(1)) region of a drift tube. As the ions approach the drift tube exit, they are exposed to a large focusing potential drop; at high fields, ions are efficiently collisionally activated and dissociate as they exit the drift tube. We have demonstrated this approach by examining the fragmentation pattern for electrosprayed bradykinin ions. These studies show that the activation process is highly tunable; it is possible to modulate the field such that precursor ion mass spectra as well as several high-field collision-induced fragmentation patterns can be obtained. The approach also appears to be a simple means of activating protein ions, as demonstrated by examining electrosprayed myoglobin ions.