Presently, many substances, such as cell receptors, hormones and immunological factors, which have measureable bioactivity are available in amounts so small that structural analysis is difficult if not impossible. The proposed research seeks to establish a new techology for the structural analysis of the rare active components isolated from biological systems. The plan is based on combining separation power of capillary zone electrophoresis with the proven analytical capabilities of liquid secondary ion mass spectrometry. Necessary increases in the sensitivity of the mass spectral analysis will be achieved through the use of a finely focused liquid metal ion beam for sample ionization. The primary ion beam will sample directly the effluent from a capillary zone electrophoresis column which will seve as the last stage of sample purification; eliminating sample handling steps which account for a majority of the material losses when working with sample amounts less than 100 pmole. If successful, a two or three orders of magnitude reduction in required sample amounts will be achieved with no sacrifice in spectral quality. Work will be directed toward the analysis of peptides and proteins but advances can be readily applied to other compound classes.
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