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Mass Difference (mass + difference)
Selected AbstractsSilicon crystal growth from the melt: Analysis from atomic and macro scalesCRYSTAL RESEARCH AND TECHNOLOGY, Issue 4-5 2005K. Kakimoto Abstract The effect of impurity concentration on thermal conductivity of natural and isotope silicon by using equilibrium molecular dynamics simulation is investigated. It was found that the concentrations of the impurities such as boron, phosphor and arsene play an important role in the propagation of phonons in silicon crystals. It was also clarified that a mass difference of impurities and host crystals results in degradation of thermal conductivity of silicon. (© 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Separation of proteins with a molecular mass difference of 2,kDa utilizing preparative double-inverted gradient polyacrylamide gel electrophoresis under nonreducing conditions: Application to the isolation of 24,kDa human growth hormoneELECTROPHORESIS, Issue 23 2005Juan J. Bustamante Abstract A method for separating proteins with a molecular mass difference of 2,kDa using SDS-PAGE under nonreducing conditions is presented. A sample mixture containing several human growth hormone (hGH) isoforms was initially separated on a weak anion-exchange column. Fractions rich in 24,kDa hGH as determined by analytical SDS-PAGE were pooled and further separated by cation-exchange chromatography. The fractions pooled from the cation-exchange chromatography contained two hGH isoforms with a 2,kDa molecular mass difference according to SDS-PAGE analysis, 22 and 24,kDa hGH. The 22 and 24,kDa hGH were separated using continuous-elution preparative double-inverted gradient PAGE (PDG-PAGE) under nonreducing conditions. The preparative electrophoresis gel was composed of three stacked tubular polyacrylamide matrices, a 4% stacking gel, a 13,18% linear gradient gel, and a 15,10% linear inverted gradient gel. Fractions containing purified 24,kDa hGH were pooled and Western blot analysis displayed immunoreactivity to antihGH antibodies. PDG-PAGE provides researchers with an electrophoretic technique to preparatively purify proteins under nonreducing conditions with molecular mass differences of 2,kDa. [source] Quantum field theories coupled to supergravityFORTSCHRITTE DER PHYSIK/PROGRESS OF PHYSICS, Issue 3 2008J. Große Abstract This article is devoted to the investigation of the interplay of supersymmetric Yang,Mills theories (SYM) and supergravity (SUGRA). The topic is studied from two points of view: Firstly from the point of view of AdS/CFT correspondence, which realises the coupling of four dimensional superconformal ,, = 4 SYM theory and ten dimensional type IIB SUGRA in a holographic way. In order to arrive at theories that resemble quantum chromodynamics (QCD) more closely, fundamental fields are introduced using probe D7-branes and non-trivial background configuration are considered. In particular supergravity solutions that are only asymptotically anti-de Sitter and break supersymmetry are used. This allows the description of spontaneous chiral symmetry breaking. The meson spectrum is calculated and the existence of an associated Goldstone mode is demonstrated. Moreover it is shown that highly radially excited mesons are not degenerate. Additionally instanton configurations on the D7-branes are investigated, which lead to a holographic description of the dual field theory's Higgs branch. Finally a holographic description of heavy-light mesons is developed, which are mesons consisting of quarks with a large mass difference, such that a treatment of B mesons can be achieved The second approach is the technique of so-called space-time dependent couplings (also known as "local couplings"), where coupling constants are promoted to external sources. This allows to explore the conformal anomaly of quantum field theories coupled to a classical gravity background. The technique is extended to the superfield description of ,, = 1 supergravity, a complete basis for the anomaly is given and the consistency conditions that arise from a cohomological treatment are calculated. Possible implications for an extension of Zamolodchikov's c -theorem to four dimensional supersymmetric quantum field theories are discussed. [source] Mass-dependent reproductive strategies in wild bighorn ewes: a quantitative genetic approachJOURNAL OF EVOLUTIONARY BIOLOGY, Issue 4 2000RÉale In the Ram Mountain bighorn sheep (Ovis canadensis) population, ewes differing by more than 30% in body mass weaned lambs with an average mass difference of only 3%. Variability in adult body mass was partly due to additive genetic effects, but inheritance of weaning mass was weak. Maternal effects could obscure genetic effects in the phenotypic expression of weaning mass, particularly if they reflected strategies of maternal expenditure that varied according to ewe mass. We performed a quantitative genetic analysis to assess genetic and environmental influences on ewe mass and on maternal expenditure. We used the mean daughters/mother regression method and Derivative Free Restricted Maximum Likelihood models to estimate heritability (h2) of ewe mass and indices of maternal expenditure. We found additive genetic effects on phenotypic variation in maternal mass, in lamb mass at weaning (absolute maternal expenditure) and in weaning mass relative to maternal mass at weaning (relative maternal expenditure). Heritability suggests that maternal expenditure has the potential to evolve. The genetic correlation of ewe mass and absolute maternal expenditure was weak, while ewe mass and relative maternal expenditure were strongly negatively correlated. These results suggest additive genetic effects on mass-dependent reproductive strategies in bighorn ewes. Mass-dependent reproductive strategies could affect lamb survival and phenotypic variation in adult mass. As population density increased and reproduction became costlier, small females reduced maternal expenditure more than large females. Constraints on reproductive strategy imposed by variations in resource availability are therefore likely to differ according to ewe mass. A general trend for a decrease in maternal expenditure relative to maternal size in mammals suggests that size-dependent negative maternal effects may be common. [source] Quantitative peptidomics of mouse pituitary: comparison of different stable isotopic tagsJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 2 2005Fa-Yun Che Abstract Determining the relative levels of neuropeptides in two samples is important for many biological studies. An efficient, sensitive and accurate technique for relative quantitative analysis involves tagging the peptides in the two samples with isotopically distinct labels, pooling the samples and analyzing them using liquid chromatography/mass spectrometry (LC/MS). In this study, we compared two different sets of isotopic tags for analysis of endogenous mouse pituitary peptides: succinic anhydride with either four hydrogens or deuteriums and [3-(2,5-dioxopyrrolidin-1-yloxycarbonyl)propyl]trimethylammonium chloride with either nine hydrogens or deuteriums. These two labels react with amines and impart either a negative charge (succinyl) or a positive charge (4-trimethylammoniumbutyryl (TMAB)). Every endogenous mouse pituitary peptide labeled with the light TMAB reagent eluted from the C18 reversed-phase column at essentially the same time as the corresponding peptide labeled with the heavy reagent. Most of the peptides labeled with succinyl groups also showed co-elution of the heavy- and light-labeled forms on LC/MS. The mass difference between the heavy and light TMAB reagents (9 Da per label) was larger than that of the heavy and light succinyl labels (4 Da per label), and for some peptides the larger mass difference provided more accurate determination of the relative abundance of each form. Altogether, using both labels, 82 peptides were detected in Cpefat/fat mouse pituitary extracts. Of these, only 16 were detected with both labels, 41 were detected only with the TMAB label and 25 were detected only with the succinyl label. A number of these peptides were de novo sequenced using low-energy collisional tandem mass spectrometry. Whereas the succinyl group was stable to the collision-induced dissociation of the peptide, the TMAB-labeled peptides lost 59 Da per H9 TMAB group. Several peptides identified in this analysis represent previously undescribed post-translational processing products of known pituitary prohormones. In conclusion, both succinyl and TMAB isotopic labels are useful for quantitative peptidomics, and together these two labels provide more complete coverage of the endogenous peptides. Copyright © 2005 John Wiley & Sons, Ltd. [source] Differentiation of sulfate and phosphate by H/D exchange mass spectrometry: application to isoflavoneJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 11 2004Akira Kanakubo Abstract Often phosphorylation or sulfation is an important step which occurs in the signal transduction and cascade of metabolic pathways. Some natural products and metabolites contain one or more sulfate or phosphate groups. Isoflavone sulfate has been identified from high-resolution mass spectrometry (HRMS) and enzymatic digestion by sulfatase. We previously reported the new water-soluble isoflavone analogs, daidzein 7- O -phosphate and genistein 7- O -phosphate, which were surprisingly hydrolyzed by sulfatase. In this previous study, we could not determine the phosphate from the results of HRMS and enzymatic digestion, that is, HRMS and enzymatic digestion did not provide clear evidence. In this case, we drew conclusions from NMR analysis. HRMS has been ineffective with a regular fast atom bombardment (FAB) mass spectrometer to distinguish between phosphate and sulfate since the mass difference is only 0.009 mass units. There was, however, no conventional method of microanalysis to distinguish phosphate from sulfate owing to the same nominal mass. It is still very difficult to determine by negative FABMS [OP(O)(OH)2] = 80 and [OS(O)2OH] = 80. In this paper, we report a method to distinguish between these groups by using a popular low-resolution mass instrument; thus, phosphate and sulfate were measured by H/D exchange mass spectrometry at the picomole level to differentiate [OP(O)(OD)2] = 82 and [OS(O)2OD] = 81, respectively. This method is applicable not only to the isoflavone, but also to other phospho and sulfo compounds. Copyright © 2004 John Wiley & Sons, Ltd. [source] ,Mass defect' tags for biomolecular mass spectrometryJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 8 2003Michael P. Hall Abstract We present a new class of ,mass defect' tags with utility in biomolecular mass spectrometry. These tags, incorporating element(s) with atomic numbers between 17 (Cl) and 77 (Ir), have a substantially different nuclear binding energy (mass defect) from the elements common to biomolecules. This mass defect yields a readily resolvable mass difference between tagged and untagged species in high-resolution mass spectrometers. We present the use of a subset of these tags in a new protein sequencing application. This sequencing technique has advantages over existing mass spectral protein identification methodologies: intact proteins are quickly sequenced and unambiguously identified using only an inexpensive, robust mass spectrometer. We discuss the potential broader utility of these tags for the sequencing of other biomolecules, differential display applications and combinatorial methods. Copyright © 2003 John Wiley & Sons, Ltd. [source] Molecular mass determination of plasma-derived glycoproteins by ultraviolet matrix-assisted laser desorption/ionization time-of-flight mass spectrometry with internal calibrationJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 11 2002Omar Belgacem Abstract Human plasma-derived antithrombin III (AT-III), factor IX (FIX) and vitronectin (VN) were characterized as native glycoproteins and in their de- N -glycosylated form by means of MALDI mass spectrometry. The average molecular masses of the three complex glycoproteins were determined applying internal calibration with high-mass, well-defined protein calibrants. Internal calibration generated for the 47 kDa yeast protein enolase a mass precision in the continuous and delayed extraction mode of ±0.12 and ±0.022%, respectively. The achievable mass accuracy for such a high-mass, unmodified protein was in the range of 0.02% in the continuous mode, which turned out to be better than in the delayed extraction mode. Purification of all (glyco) proteins (even the calibration proteins) by means of ZipTip® technology and direct elution with a solvent system containing the appropriate MALDI matrix turned out to be a prerequisite to measure the exact molecular masses with an internal calibration. The average molecular masses of the two different forms of AT-III, namely AT-III, and AT-III,, were shown to be 57.26 and 55.04 kDa, respectively. The 2.22 kDa mass difference is attributed to the known difference in carbohydrate content at one specific site (Asn-135). After exhaustive de- N -glycosylation (by means of PNGase F) of the ,- and ,-form and subsequent MALDI-MS analysis, average molecular masses of 48.96 and 48.97 kDa, respectively, were obtained. These values are in good agreement (,0.15%) with the calculated molecular mass (49.039 kDa) of the protein part based on SwissProt data. The molecular mass of the heavily post-translational modified glycoprotein FIX was found to be 53.75 kDa with a peak width at 10% peak height of 4.5 kDa, because of the presence of many different posttranslational modifications (N - and O -glycosylation at multiple sites, sulfation, phosphorylation, hydroxylation and numerous ,-carboxyglutamic acids). MALDI-MS molecular mass determination of the native, size-exclusion chromatography-purified, VN sample revealed that the glycoprotein was present as dimer with molecular mass of 117.74 kDa, which could be corroborated by non-reducing SDS-PAGE. After sample treatment with guanidine hydrochloride and mass spectrometric analysis, a single, new main component was detected. The molecular mass turned out to be 59.45 kDa, representing the monomeric form of VN, known as V75. The determined molecular mass value was shown to be on one hand lower than from SDS-PAGE and on the other higher than the calculated amino acid sequence molecular mass (52 277 Da), pointing to the well-known SDS-PAGE bias and to considerable post-translational modifications. Further treatment of the sample with a reducing agent and subsequent MALDI-MS revealed two new components with molecular masses of 49.85 and 9.41 kDa, corresponding to V65 and V10 subunits of VN. PNGase F digest of the V75 and V65 units and MS analysis, exhibiting a molecular mass reduction of 6.37 kDa in both cases, verified the presence of a considerable amount of N -glycans. Copyright © 2002 John Wiley & Sons, Ltd. [source] Matrix-assisted laser desorption/ionization Fourier transform mass spectrometric analysis of oxygenated triglycerides and phosphatidylcholines in egg tempera paint dosimeters used for environmental monitoring of museum display conditionsJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 5 2001Oscar F. van den Brink Abstract Oxidative changes in triacylglycerols and diacylphosphatidylcholines in egg tempera paint strips are used for chemical dosimetry of the quality of the museum environment. High-resolution matrix-assisted laser desorption/ionization Fourier transform mass spectrometry (MALDI-FTMS) was used as a rapid method for the determination of the exact elemental composition of the alteration products from diacylphosphatidylcholines and triacylglycerols. Light exposure of the egg tempera paints yields oxygenated diacylphosphatidylcholines and triacylglycerols. In the latter multiple incorporation of oxygen was observed as a recurring mass difference of 15.995, the exact atomic mass of oxygen. Owing to the high resolution of the FTMS data (routinely 20 000 at m/z 1000 in broadband mode), oxidation products with different elemental compositions but identical nominal mass could be distinguished. Products of oxidative cleavage of triacylglycerols were observed in samples exposed for longer times. The relative intensities of the peaks of singly and multiply oxygenated triacylglycerols were used to derive the degree of oxygenation of the egg lipids in the tempera paint dosimeters. The degree of oxygenation was found to be directly related to the light exposure time. Exposure to elevated temperature (60 °C) for a period of 21 days did not lead to oxygenation of the triacylglycerols and diacylphosphatidylcholines. Exposure to NOx and SO2 in the dark greatly increased the degree of oxygenation. Addition of lead- or copper-containing pigments to the egg binding medium (and subsequent storage for 6 months in the dark) led to accelerated conversion of egg lipids to oxidised products. Copyright © 2001 John Wiley & Sons, Ltd. [source] Sequence and phosphorylation level determination of two donkey , -caseins by mass spectrometryRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 13 2009Vincenzo Cunsolo Two coeluting components, with experimentally measured Mr values of 25529 and 24606 Da, were identified by reversed-phase high-performance liquid chromatography (RP-HPLC) and mass spectrometric analysis in the dephosphorylated casein fraction of a milk sample collected from an individual donkey belonging to the Ragusano breed of the east of Sicily. By coupling enzymatic digestions, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and RP-HPLC/nano-electrospray ionization tandem mass spectrometry (nESI-MS/MS) analysis, the two proteins were identified as donkey , -CNs and their sequences characterized completely, using the two known , -CNs from mare as references. The two donkey , -CNs, showing a mass difference of 923 Da, differ by the presence of the domain E27SITHINK34 in the full-length component (Mr 25529 Da). In comparison with the mare's , -CNs used as reference, they present nine amino acid substitutions: L,S37, R,H52, S,N81, P,V84, L,V91, R,Q203, P,L/I206, L,F210 and A,P219. Together, these substitutions account for the increase of 18 Da in the Mr of the donkey , -CNs with respect to the counterparts from the mare. The molecular mass determination by ESI-MS for the phosphorylated proteins showed that the full-length component was composed of highly multi-phosphorylated isoforms with five to seven phosphate groups. By analogy with the homologous mare's , -CNs, the full-length (226 amino acids) , -CN was termed variant A, whereas the shorter (218 amino acids) , -CN was termed variant A,5. Copyright © 2009 John Wiley & Sons, Ltd. [source] Metabolite identification of small interfering RNA duplex by high-resolution accurate mass spectrometryRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 12 2008Yan Zou On-line liquid chromatography/electrospray ionization high-resolution mass spectrometry (LC/ESI-HRMS) using an LTQ-Orbitrap mass spectrometer was employed to investigate the metabolite profiles of a model siRNA duplex designated HBV263. The HBV263 duplex was incubated in rat and human serum and liver microsomes in vitro. The siRNA drug and its metabolites were then extracted using a liquid-liquid extraction followed by solid-phase extraction (LLE-SPE), and analyzed by LC/ESI-MS. High-resolution accurate mass data enabled differentiation between two possible metabolite sequences with a monoisotopic molecular mass difference of less than 1,Da. ProMass deconvolution software was used to provide semi-automated data processing. In vitro serum and liver microsome incubation samples afforded different metabolite patterns: the antisense strand of the duplex was degraded preferentially in rat and human serum, while the sense strand of the duplex was less stable in rat and human liver microsomes. Copyright © 2008 John Wiley & Sons, Ltd. [source] Derivatization for liquid chromatography/electrospray mass spectrometry: synthesis of tris(trimethoxyphenyl)phosphonium compounds and their derivatives of amine and carboxylic acidsRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 5 2002William J Leavens A simple method for the derivatization of primary amines and carboxylic acids with tris(trimethoxyphenyl)phosphonium (TMPP) reagents to enhance their detection by electrospray mass spectrometry (ESI-MS) has been developed. The synthesis of novel TMPP reagents and their stable isotopically labelled analogues is described. Through the use of stable isotopically labelled TMPP ,tags', incorporation of a doublet (1:1, 1H/2H or 12C/13C) into the target molecule can be achieved, enabling the use of isotopic target analysis to detect compounds of unknown molecular weight but with a characteristic isotope pattern and accurate mass difference. Copyright © 2002 John Wiley & Sons, Ltd. [source] Separation of proteins with a molecular mass difference of 2,kDa utilizing preparative double-inverted gradient polyacrylamide gel electrophoresis under nonreducing conditions: Application to the isolation of 24,kDa human growth hormoneELECTROPHORESIS, Issue 23 2005Juan J. Bustamante Abstract A method for separating proteins with a molecular mass difference of 2,kDa using SDS-PAGE under nonreducing conditions is presented. A sample mixture containing several human growth hormone (hGH) isoforms was initially separated on a weak anion-exchange column. Fractions rich in 24,kDa hGH as determined by analytical SDS-PAGE were pooled and further separated by cation-exchange chromatography. The fractions pooled from the cation-exchange chromatography contained two hGH isoforms with a 2,kDa molecular mass difference according to SDS-PAGE analysis, 22 and 24,kDa hGH. The 22 and 24,kDa hGH were separated using continuous-elution preparative double-inverted gradient PAGE (PDG-PAGE) under nonreducing conditions. The preparative electrophoresis gel was composed of three stacked tubular polyacrylamide matrices, a 4% stacking gel, a 13,18% linear gradient gel, and a 15,10% linear inverted gradient gel. Fractions containing purified 24,kDa hGH were pooled and Western blot analysis displayed immunoreactivity to antihGH antibodies. PDG-PAGE provides researchers with an electrophoretic technique to preparatively purify proteins under nonreducing conditions with molecular mass differences of 2,kDa. [source] Seasonal changes in herbage mass and nutritive value of a range of grazed legume swards under Mediterranean and cool temperate conditionsGRASS & FORAGE SCIENCE, Issue 3 2007U. Sölter Summary Seasonal changes in herbage mass and herbage quality of legume-based swards under grazing by sheep or cattle were investigated at four locations in climatically different zones of Europe: Sardinia (Italy), southern France, northern Germany and south-west England (UK). At each location standard treatments were applied to legumes typical of species widely used in each locality: Medicago polymorpha in Italy, Medicago sativa in France, and Trifolium repens in Germany and in UK. At each site comparisons were made of two other legumes: Trifolium subterraneum and Hedysarum coronarium in Italy, Onobrychis sativa and Trifolium incarnatum in France, Trifolium pratense and Lotus corniculatus in Germany, and Trifolium ambiguum and L. corniculatus in UK. Legumes were sown in mixture with locally appropriate companion grasses, and measurements were made over two or three grazing periods. In Italy M. polymorpha swards gave the greatest herbage mass in grazing period 1 but H. coronarium was more persistent. At the French site all legumes established poorly with no significant herbage mass differences between treatments. At both the UK and German sites L. corniculatus maintained a high proportion of legume in the sward; T. repens showed poor persistence under continuous sheep grazing in UK but persisted under cattle grazing in Germany, while T. ambiguum was slow to establish in the UK, and T. pratense proved to be of comparable herbage mass to the standard T. repens -based sward in the last year of the experiment. The concentration of crude protein and in vitro digestibility of organic matter in the dry matter of herbage showed greater within-season variation than between treatments at each site. It is concluded that, in addition to currently used species, legume-based swards containing H. coronarium, O. sativa and L. corniculatus all have potential to contribute to forage production for low-input grazing and their use merits further consideration in systems of livestock production in Europe. [source] Neutral loss of amino acid residues from protonated peptides in collision-induced dissociation generates N- or C-terminal sequence ladders,JOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 11 2003Mogjiborahman Salek Abstract The widespread occurrence of the neutral loss of one to six amino acid residues as neutral fragments from doubly protonated tryptic peptides is documented for 23 peptides with individual sequences. Neutral loss of amino acids from the N-terminus of doubly charged tryptic peptides results in doubly charged y-ions, forming a ladder-like series with the ions [M + 2H]2+ = ymax2+, ymax , 12+, ymax , 22+, etc. An internal residue such as histidine, proline, lysine or arginine appears to favor this type of fragmentation, although it was sometimes also observed for peptides without this structure. For doubly protonated non-tryptic peptides with one of these residues at or near the N-terminus, we observed neutral loss from the C-terminus, resulting in a doubly charged b-type ion ladder. The analyses were performed by Q-TOF tandem mass spectrometry, facilitating the recognition of neutral loss ladders by their 2+ charge state and the conversion of the observed mass differences into reliable sequence information. It is shown that the neutral loss of amino acid residues requires low collision offset values, a simple mechanistic explanation based on established fragmentation rules is proposed and the utility of this neutral loss fragmentation pathway as an additional source for dependable peptide sequence information is documented. Copyright © 2003 John Wiley & Sons, Ltd. [source] Screening strategy for the rapid detection of in vitro generated glutathione conjugates using high-performance liquid chromatography and low-resolution mass spectrometry in combination with LightSight® software for data processingRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 22 2009César Ramírez-Molina The knowledge of drug metabolism in the early phases of the drug discovery process is vital for minimising compound failure at later stages. As chemically reactive metabolites may cause adverse drug reactions, it is generally accepted that avoiding formation of reactive metabolites increases the chances of success of a molecule. In order to generate this important information, a screening strategy for the rapid detection of invitro generated reactive metabolites trapped by glutathione has been developed. The bioassay incorporated the use of native glutathione and its close analogue the glutathione ethyl ester. The generic conditions for detecting glutathione conjugates that undergo constant neutral loss of 129 Da were optimised using a glutathione-based test mix of four compounds. The final liquid chromatography/tandem mass spectrometry constant neutral loss method used low-resolution settings and a scanning window of 200 amu. Data mining was rapidly and efficiently performed using LightSight® software. Unambiguous identification of the glutathione conjugates was significantly facilitated by the analytical characteristics of the conjugate pairs formed with glutathione and glutathione ethyl ester, i.e. by chromatographic retention time and mass differences. The reliability and robustness of the screening strategy was tested using a number of compounds known to form reactive metabolites. Overall, the developed screening strategy provided comprehensive and reliable identification of glutathione conjugates and is well suited for rapid routine detection of trapped reactive metabolites. This new approach allowed the identification of a previously unreported diclofenac glutathione conjugate. Copyright © 2009 John Wiley & Sons, Ltd. [source] Extracting metabolite ions out of a matrix background by combined mass defect, neutral loss and isotope filtrationRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 2 2009Filip Cuyckens Mass defect, neutral loss and isotope filtration techniques were applied to electrospray ionization mass spectrometry (ESI-MS) data obtained for in vivo and in vitro samples of drug metabolism studies. A combination of these post-acquisition processing techniques was shown to be more powerful than the use of one of these tools alone for the detection in complex matrices of metabolites of candidate drugs with a characteristic isotope pattern (e.g. containing bromine, chlorine, or a high proportion of radiolabeled drug (12C/14C)) or characteristic neutral losses. In combination with ,all-in-one' data acquisition this methodology is able to perform software-driven constant neutral loss scanning for an unlimited number of mass differences at any time after analysis. Highly selective MS chromatograms were obtained with excellent correlation with their corresponding radiochromatograms. Copyright © 2009 John Wiley & Sons, Ltd. [source] | ||||||||||||||||