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Identification of peptides

Li, J., Kelly, J.F., Chernushevich, I., Harrison, D.J., and Thibault P., Separation and identification of peptides from gel-isolated membrane proteins using a microfabricated device for combined capillary electrophoresis/nanoelectro-spray mass spectrometry, Anal. Chem. 72, 599, 2000. [Pg.437]

Mann, M. Wilm, M. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem. 1994, 66,4390-4399. [Pg.274]

Toll, H., Oberacher, H., Swart, R., Huber, C.G. (2005). Separation, detection, and identification of peptides by ion-pair reversed-phase high-performance hquid... [Pg.175]

Cargile, B. J., Stephenson, J.L., Jr. (2004). An alternative to tandem mass spectrometry isoelectric point and accurate mass for the identification of peptides. Anal. Chem. 76, 267-275. [Pg.256]

Udupa, P.E., and Sharma, K.K. (2005) Effect of oxidized betaB3-crystallin peptide (152-166) on thermal aggregation of bovine lens gamma-crystallins identification of peptide interacting sites. Exp. Eye. Res. 80(2), 185-196. [Pg.1123]

M. Mann and M. Wilm. Error-Tolerant Identification of Peptides in Sequence Databases by Peptide Sequence Tags. Anal. Chem., 66(1994) 4390-4399. [Pg.80]

The identification of peptides and proteins using MS information can be done in three different fashions (i) de novo sequencing, (ii) library searching, and (iii) sequence collection searching. [Pg.213]

J. Couet, S. Li, T. Okamoto, T. Izeku, and M. P. Lisanti. Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J. Biol. Chem. 272 6525-6533... [Pg.612]

The literature contains numerous references to the use of MS/MS in the determination of new neuropeptides in identified cells of invertebrates (Bulau et al., 2004, for a recent example) and this technique is now being applied to in situ analysis of vertebrate tissues (Fournier et al., 2003). MS/MS is also used for studies of neuropeptide processing (Nilsson et al., 2001), pharmacokinetics of synthetic peptides (Mock et al., 2002), nonpeptide drug metabolism (Kamel et al., 2003), identification of peptides purified by immunoaffinity (Suresh Babu et al., 2004), and MALDI/MS/MS techniques adaptable to brain dialysis (Bogan and Agnes, 2004). [Pg.156]

Libraries can also be made from naturally occurring peptides (e.g. melanocortin [30] and somatostatin [31]) and their variants, or be derived from protein-fragments. The former have been employed mainly for the identification of peptide variants with unproved characteristics, and the latter for the identification of antigenic determinants present on targets, for example by selecting for binders to monoclonal antibodies specific for an antigen-fragment peptide library. [Pg.260]

Naturally occurring peptides can be altered in size and structure, and randomization of residues can be introdnced into libraries for the identification of peptides with improved characteristics or improved binding specificity. Snch an approach has been used to select re-ceptor-spedfic variants of atrial natrinretic peptide (ANP) with improved expression in E. coli and spedficity for jnst one form of the ANP receptors [29]. [Pg.260]

Phage displayed peptide libraries have been snccessfnlly employed for the identification of peptide ligands with a variety of applications. Recent reviews describe the developments in the generation and screening of peptide libraries [6], their application in the identification of receptor ligands [32] and in drng development [33]. [Pg.260]

Ehrlich, G.K. and Bailon, R, Identification of peptides that bind to the constant region of a humanized IgGi monoclonal antibody using phage display, J. Mol. Recogn., 11, 121-125, 1998. [Pg.382]

Isolation and identification of peptides formed during beef... [Pg.584]

Sufficient mass accuracy this is important particularly in the case of identification of peptides by comparison with real database values. [Pg.107]

Alii, I., Kokoniewska, M., Gibbs, B. F., and Konishi, Y. (1998). Identification of peptides in Cheddar cheese by electrospray ionization mass spectrometry. Int. Dairy. 8, 643-649. [Pg.201]

McSweeney, P. L. H., Pochet, S., Fox, P. F., and Healy, A. (1994). Partial identification of peptides from water-insoluble fraction of Cheddar cheese. J. Dairy Sci. 61, 587-590. [Pg.209]

Sousa, M. J. and Malcata, F. X. (1998). Identification of peptides from ovine milk cheese manufactured with animal rennet or extracts of Cynara cardunculus as coagulant. J. Agric. Food Chem. 46, 4034-4041. [Pg.211]

Swiderek, K. M. Davis, M. T. Lee,T. D. 1998. The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses. Electrophoresis, 19,989-997. [Pg.228]

Traditional biochemical techniques such as liquid chromatography (LC), gel electrophoresis, capillary electrophoresis (CE), and mass spectrometry (MS) have been widely used for the complete analysis of salivary proteins and peptides. The recent advances in these technical approaches applied to peptidomics have allowed a better comprehensive analysis of peptides in human whole saliva, envisioning the identification of potential salivary biomarkers of oral and systemic diseases. Sample preparation is a critical experimental step for the successful identification of peptides using MS-based approaches, for their quantitation and identification of PTMs. [Pg.224]

Machtejevas E, John H, Wagner K, Standker L, Marko-Varga G, Forssmann WG, Bischoff R, Unger KK (2004) Automated multi-dimensional liquid chromatography sample preparation and identification of peptides from human blood filtrate. J Chromatogr B 803 121-130... [Pg.346]


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See also in sourсe #XX -- [ Pg.106 , Pg.107 ]




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