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12:10 The derivatized amino acids are separated in 5-mM carbonate buffer at pH 10, on a 50-mm i.d. fused silica capillary of 99 cm length, with a 25-kV separation potential. Electrokinetic injection is performed at the anodic end of the capillary, with a 2-kV injection potential applied for 10 s. Figure 12.4 shows a schematic diagram of the laser-induced uorescence detector. The fused silica capillary used for electrophoresis is placed $ 1 cm into the ow chamber of the sheath ow cuvette. The sheath stream surrounds the sample as it exits from the capillary, forming a thin stream in the center of the ow chamber. A focused laser beam (not shown) excites uorescence. The uorescence is collected at right angles, with a microscope objective, and passed through lters (cutting off radiation < 495 nm and > 560 nm), to reduce Raman and Rayleigh scattered light, and passed through an eyepiece tted with a 200-mm radius pinhole. The pinhole restricts the eld of view of the photomultiplier tube (PMT) detector to the illuminated sample stream. Precise alignment of the laser beam, objective, eyepiece pinhole, and PMT are required for the detection of maximum sample emission. The stainless steel body of the cuvette and the associated plumbing are held at ground potential. Figure 12.5 shows an electropherogram recorded by this detector after the injection and separation of a mixture of 15 FITC-derivatized amino acids, and
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Figure 12.4. Laser-induced uorescence detector for CZE. [Reprinted, with permission, from Y.-F. Cheng and N. J. Dovichi, Science 242, 1988, 562 564. Subattomole Amino Acid Analysis by Capillary Zone Electrophoresis and Laser-Induced Fluorescence . Copyright # 1988 by AAAS.
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Figure 12.5. Data obtained with the LIF detector for 15 amino acids.4 [Reprinted, with permission, from Y.-F. Cheng and N. J. Dovichi, Science 242, 1988, 562 564. Subattomole Amino Acid Analysis by Capillary Zone Electrophoresis and Laser-Induced Fluorescence . Copyright # 1988 by AAAS.]
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Table 12.2 below indicates detection limits observed for each amino acid. While the detection of amino acids is not in itself of particular interest, peptides and proteins that are available only in very small quantities may be analyzed for their amino acid contents, following acid hydrolysis, using the instrumentation described here.
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TABLE 12.2. Detection Limits Observed for Each Amino Acida Amino Acid Ala Arg Asp Cys Glu Gly Ile Leu Lys Met Ser Thr Trp Tyr Concentration ( 10 11 M) 3.4 <0.5 6.6 2.4 2.6 2.8 1.7 7.0 8.6 1.6 1.6 2.6 1.1 1.1 Mole ( 10 20) 4.6 <0.9 6.8 3.3 2.8 3.7 2.5 10 15 2.3 2.3 3.7 1.7 1.4 Molecules 27,000 <5,700 41,000 20,000 17,000 22,000 15,000 61,000 90,000 14,000 13,000 22,000 9,900 8,400
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a Reprinted, with permission, from J. B. Fenn, M. Mann, C. K. Meng, S. F. Wong, and C. M. Whitehouse, Science 246, 1989, 64 71. Electrospray Ionization for Mass Spectrometry of Large Biomolecules . Copyright # 1989 by AAAS.
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12.5.2. Mass Spectrometric Detection Mass spectrometric detectors for capillary electrophoresis are necessarily postcolumn detectors and must be interfaced to the cathodic end of the capillary. These detectors consist of four main components: the interface, that joins the capillary to the ion source, the ion source, that generates ionic fragments from neutral analyte species, the mass analyzer, that distinguishes ions by their mass/charge (m/z) values, and the ion detector, that measures and ampli es the signal. The principles and instrumentation of bioanalytical MS are explained in 15. Soft ionization methods produce few fragments under relatively mild conditions. The ionization method that has received the most attention in terms of its applicability to protein and DNA analysis is the electrospray ionization (ES) technique. This is a soft method that is capable of generating molecular ions from biological macromolecules present in solution. Table 12.3 gives examples of the charge and m/z ranges that have been observed with some biopolymer species in electrospray ionization mass spectrometers. Because of the range of m/z values produced by species of constant mass, sophisticated software has been developed for data reduction with ES MS, allowing the molecular weights of macromolecules to be determined with very high precision and accuracy. Because the molecular weights are so large, the natural abundances of the isotopes must be considered when analyzing m/z data. Signals for a single parent species are observed over a range of m/z values because of this isotopic distribution. These topics are considered in 15. ES MS has been interfaced to the cathodic end of capillaries used for capillary electrophoresis. Figure 12.6 shows a diagram of a typical instrumental apparatus, while Figure 12.7 shows a detailed schematic of one type of capillary ionization source interface. The design of the interface is critical, and has been a very active area of research. With the device shown in Figure 12.7, the operational parameters are as follows. The separation potential, applied between the anodic and cathodic ends of the capillary, are between 30 and 50 kV, and the cathode is maintained at $ 3 6 kV above ground. The focusing ring is maintained at 300 V, while the ion-sampling nozzle and skimmer are grounded. This electrical arrangement ensures ion formation and acceleration into the magnetic sector.
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TABLE 12.3. Charges and m=z Values Obtained for Biological Macromolecules using ES MSa Compound Insulin Cytochrome c Alcohol dehydrogenase (subunit) Conalbumin Oligonucleotide (CATGCCATGGCATG)
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