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By Morse M., Littauer S. B.

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The protein field, including automated digestion robots. In a final section we discuss peptide sample preparation techniques for obtaining optimal analytical results, including MALDI (matrix-assisted laser desorption ionization) and ES (electrospray) purification and concentration methods using chromatographic material. 1. Secondary elution/concentration gel electrophoresis Although modem biological mass spectrometry is currently becoming the method of choice for the identification of gel-separated proteins, classical methods such as chemical Edman sequencing are still very much applied in the protein field.

Overall automation attempts in the protein digestion field wi111ead to further developments. 3. 1 Preparation of biological samples for MALDI-MS analysis MALDI mass spectrometry has over the past few years evolved to a powerful analytical technique for the characterization of the primary structure of peptides and proteins. Several approaches have been described for this purpose [9], of which peptide mass fingerprinting and post-source-decay (PSD) analysis are mainly employed. The preparation of MALDI samples seems very simple.

The samples are either spotted from a robot needle tip or are spotted with a capillary nozzle tool or ink jet set-up. g. at the MPI for Molecular Genetics in Berlin, by sputtering the sample on a small target size using a system similar to that used in ink jet printers, thus allowing thousands of spots to be loaded on a single small MALDI target. For any type ofMALDI target, almost every existing robot platform can be upgraded for this kind of work, and they appear on the market under diverse commercial names.

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A Characterization of Fields in the Calculus of Variations by Morse M., Littauer S. B.

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