Peptide by liquid chromatography

D Agostino PA, Hancock JR, Provost LR. 1997. Analysis of bioactive peptides by liquid chromatography-high-resolution electrospray mass spectrometry. J Chromatogr... 

Newcomb, R. (1992). High-sensitivity detection of peptides by liquid chromatography using postcolumn derivatization with fluorescamine. LC-GC 10(1), 34-39. 

Van den Broek I, Sparidans RW, Schellens JH, Beijnen JH. Quantitative bioanalysis of peptides by liquid chromatography coupled to (tandem) mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 2008 872(1—2) 1—22. 

Briefly, the workflow for these determinations is as follows preparation of a protein sample, parallel treatments of reduced and unreduced samples with iodoacetamide, digestion of proteins with trypsin, and analysis of peptides by Liquid Chromatography coupled with Mass Spectrometry (LC-MS). 

Rauniyar, N., Stevens, S.M., Prokai-Tatrai, K., Prokai, L. (2009) Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition neutral loss-driven MS versus neutral loss-driven electron capture dissociation. Analytical Chemistry, 81,782-789. 

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 5.11. Generic approaches to identify interacting proteins within complexes. The complex is isolated from cells by affinity purification using a tag sequence attached to a protein known to be in the complex. Alternatively, the complex can be immunprecipitated with an antibody to one of the proteins in the complex. The proteins are resolved by polyacrylamide gel electrophoresis, proteolyzed, and the mass of the resulting peptides is determined by mass spectrometry. Alternatively, the proteins can be proteolyzed and the resulting peptides resolved by liquid chromatography. The peptide masses are then determined by mass spectrometry and used for database searching to identify the component proteins.

U. Kertscher, M. Beyermann, E. Krause, J. Furkert, H. Berger, M. Bienert, B. Mehlis, The Degradation of Corticotropin-Releasing Factor by Enzymes of the Rat Brain Studied by Liquid Chromatography-Mass Spectrometry , Peptides 1998, 19, 649-658. 

Marquez CD, Weintraub ST, Smith PC. 1997. Quantitative analysis of two opiod peptides in plasma by liquid chromatography-electrospray ionization tandem mass spectrometry. J Chromatogr Biomed Sci Appl 694 21. 

Colistin is a linear-ring peptide antibiotic. Its main components are colistin A and colistin B. It is a member of the polymyxin family of antibiotics that is stable in dry form and in water solution. The sulfate salt of colistin, which is usually administered as feed additive, is soluble in water, slightly soluble in methanol, and practically insoluble in acetone and ether. Colistin components do not have any specific fluorophore and UV chromophore, so detection by liquid chromatography at residue levels of interest is difficult without including a suitable derivatization step in the analytical method. 

JC Scherz, JC Monti, R Jost. Analysis of the peptide sweetener aspartame by liquid chromatography. Z Lebensm Unters Forsch 177 124-128, 1983. 

Zhang F, Bartels MJ, Stott WT Quantitation ofhuman glutathione S-transferases in complex matrices by liquid chromatography/tandem mass spectrometry with signature peptides. Rapid Commun. Mass Spectrom. (2004) 18 491 98. 

TABLE 2 Mass Spectrometric Approaches for Peptide Identification After Separation By Liquid Chromatography Including Relative Performance Comparisons... 

John H, Walden M, Schafer S, Genz S, Forssmann WG (2004) Analytical procedures for peptide quantification in pharmaceutical research by liquid chromatography-mass spectrometry. Anal Bioanal Chem 378 883-897... 

Proteins are separated by one-dimensional, or more often, two-dimensional gel electrophoresis. The separated proteins are subjected to in situ tryptic digestion, and the peptides are separated by liquid chromatography and identified by mass spectrometry. See Nishihara, J.C. and Champion, K.M., Quantitative evaluation of proteins in one- and two-dimensional polyacrylamide gels using a fluorescent stain, Electrophoresis 23, 2203-2215, 2002. 

De Person, M., Sevestre, A., Chaimbault, P., Perrot, L., Duchiron, F., and Elfakir, C. (2004) Characterization of low-molecular weight peptides in champagne wine by liquid chromatography/tandem mass spectrometry, Anal. Chim. Acta, 520, 149-158. 

Czerwenka, C., Zhang, M. M., Kaehlig, H., Maier, N. M., Lipkowitz, K. B., Lindner,W. Chiral Recognition of Peptide Enantiomers by Cinchona Alkaloid Derived Chiral Selectors Mechanistic Investigations by Liquid Chromatography, NMR Spectroscopy, and Molecular Modeling, J. Org. Chem., 2003, 68, 8315-8327. 

Figure 1.2 The classical continuous labeling (bottom-up) HX-MS experiment. HX of an equilibrated protein solution is initiated by dilution into a Dfl-containing buffer, and exchange is quenched at various time points. Global HX (protein level) can be measured directly by liquid chromatography (LC) and mass spectrometry (MS) analysis of the intact protein, or local HX (peptide level) can be measured by enzymatic cleavage and subsequent LC-MS analysis of the proteolytic peptides. (See insert for color representation of the figure.)...

Kawakami H, Ohtsuki S, Kamiie J, Suzuki T, Abe T, Terasaki T (2011) Simultaneous absolute quantification of 11 cytochrome P450 isoforms in human liver microsomes by liquid chromatography tandem mass spectrometry with in silico target peptide selection. J Pharm Sci 100 341-352... 

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