Total-ion current

The total ion current (TIC) can either be measured by a hardware TIC monitor before mass analysis, or it can be reconstructed by the data system from the spectra after mass analysis. [27] Thus, the TIC represents a measure of the overall intensity of ion production or of mass spectral output as a function of time, respectively. The TIC obtained by means of data reduction, [28] i.e., by mathematical construction from the mass spectra as successively acquired while the sample evaporates, is also termed total ion chromatogram (TIC). For this purpose, the sum of all ion intensities belonging to each of the spectra is plotted as a function of time or scan number, respectively. 

Note Modem instmments usually do not support hardware TIC measurements, but including the mass spectrometers of the 1970s, there used to be a hardware TIC monitor, i.e., an ampere meter on the electronics panel. The TIC was obtained by measuring the ion current caused by those ions hitting the ion source exit plate instead of passing through its slit. 

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Once the mass spectral information has been acquired, various software programs can be employed to print out a complete or partial spectrum, a raw or normalized spectrum, a total ion current (TIC) chromatogram, a mass chromatogram, accurate mass data, and metastable or MS/MS spectra. 

Total ion current (TIC), (a) After mass analysis the sum of all the separate ion currents carried by the different ions contributing to the spectrum, (b) Before mass analysis the sum of all the separate ion currents for ions of the same sign. 

A book (B-71MS) and a review by Nishiwaki (74H(2)473) contain much information about the behaviour of pyrazoles under electron impact. The Nishiwaki review covers mainly the hydrogen scramblings and the skeletal rearrangements which occur. One of the first conclusions reached was that pyrazoles, due to their aromatic character, are extremely stable under electron impact (67ZOR1540). In the dissociative ionization of pyrazole itself, the molecular ion contributes about 45% to the total ion current thus, the molecular ion is the most intense ion in the spectrum. 

Contrary to popular opinion, slow injection of a large sample (3-5 pt ) by split injection is best. The mass spectrometer total ion current will return to the baseline more quickly using a slow injection technique. 

Total ion current (TIC) The sum of all the separate ion currents contributed by the ions that make up the spectrum. 

It is particularly difficult to study charge transfer reactions by the usual internal ionization method since the secondary ions produced will always coincide with ions produced in primary ionization processes. Indeed these primary ions frequently constitute the major fraction of the total ion current, and the small intensity changes originating from charge transfer reactions are difficult to detect. For example, Field and Franklin (5) were unable to detect any charge transfer between Xe + and CH4 by the internal ionization method although such reactions have been observed using other techniques (3, 9,22). 

Figure 5. Total ion current from different gases measured on blanked-off first electrode. Rare gases show much lower negative currents. Negative current deficiency believed caused by electrons...

From a mass spectrometry perspective, the pump must be pulse free, i.e. it must deliver the mobile phase at a constant flow rate. Pulsing of the flow causes the total ion current (TIC) trace (see Chapter 3) - the primary piece of information used for spectral analysis - to show increases in signal intensity when analytes are not being eluted and this makes interpretation more difficult. 

The fundamental piece of information on which the subsequent spectral analysis is based is the total-ion-current (TIC) trace. Such a trace, obtained from the LC-MS analysis of a pesticide mixture, is shown in Figure 3.13, together with the UV trace recorded simultaneously. For the purposes of this discussion, the HPLC and MS conditions used to generate the data, other than the fact that electrospray ionization was used, are irrelevant. 

If the belt moves too quickly, in relation to the rate of deposition, sample will not be deposited on all parts of the belt. This results in the production of an uneven total-ion-current (TIC) trace and a distortion of the mass spectra obtained, with consequent problems in interpretation, particularly if library searching is employed. 

Assuming the sequence of the parent protein is known, it is not necessary to redetermine the whole sequence merely to locate, and sequence, that/those polypeptide(s) that have undergone modification. This can be done by examination of the total-ion-current (TIC) trace before and after protein hydrolysis for the appearance of new polypeptides or to use mass spectrometry methodology to locate those polypeptides that contain certain structural features. Examples are provided here of both methodologies. 

Figure 5.27 Selective detection of lactolated peptides from a tryptic digest of / -lacto-globulins by LC-electrospray-MS-MS, showing (a) the total-ion-cnrrent trace in full-scan mode, and (b) the total-ion-current trace in neutral-loss-scanning mode. Figure from Selective detection of lactolated peptides in hydrolysates by liquid chromatography/ electrospray tandem mass spectrometry , by Molle, D., Morgan, F., BouhaUab, S. and Leonil, J., in Analytical Biochemistry, Volume 259, 152-161, Copyright 1998, Elsevier Science (USA), reproduced with permission from the publisher.

Figure 5.41 The total-ion-current (TIC) trace and reconstructed ion chromatograms from the predicted pseudomolecular ions of Indinavir m/z 614) and its mono- (m/z 630) and dihydroxy metabolites (m/z 646), generated from full-scan LC-MS analysis of an incubation of Indinavir with rat liver S9. Reprinted by permission of Elsevier Science from Identification of in vitro metabolites of Indinavir by Intelligent Automated LC-MS/MS (INTAMS) utilizing triple-quadrupole tandem mass spectrometry , by Yu, X., Cui, D. and Davis, M. R., Journal of the American Society for Mass Spectrometry, Vol. 10, pp. 175-183, Copyright 1999 by the American Society for Mass Spectrometry.

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