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A comparative study of enantioseparations was performed in capillary liquid chromatography (CLC) and capillary electrochromatography (CEC). Cellulose tris(3,5‐Dichlorophenylcarbamate) (CDCPC) was used as stationary phase in combination with nonaqueous liquid phases. Laser light scattering and scanning electron microscopic techniques were used in order to characterize the packing material. Van Deemter curves were plotted and the A, B, and C coefficients were calculated in order to determine the contribution of the various band‐broadening increments of the plate height in CLC and CEC.

A simple and rapid strategy is described to screen protein fractions for defined enzymatic activity. A protein fraction from a porcine kidney extract was immobilized by covalent coupling to activated affinity beads. The immobilized proteins were incubated with probes specific for different enzyme activities. The reaction products were analyzed by matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry. The MALDI spectra indicate the presence of 5'-nucleotidase, phosphatase, kinase, glutathione reductase, and renin activities in the kidney protein extract. Furthermore, the method can be used to screen for inhibitors of enzymatic reactions. The method is adaptable to high-throughput sample handling and automated mass spectrometric analysis and therefore suited for functional genomics. Copyright 2001 Academic Press.