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Mass spectrometry sequencing

Table 5.7 Theoretically predicted polypeptides from the trypsin digestion of S-lacto-globulin (/3LG) . Reprinted from J. Chromatogr., A, 763, Turula, V. E., Bishop, R. T., Ricker, R. D. and de Haseth, J. A., Complete structure elucidation of a globular protein by particle beam liquid chromatography-Fourier transform infrared spectrometry and electrospray liquid chromatography-mass spectrometry - Sequence and conformation of /3-lactoglobulin , 91-103, Copyright (1997), with permission from Elsevier Science... Table 5.7 Theoretically predicted polypeptides from the trypsin digestion of S-lacto-globulin (/3LG) . Reprinted from J. Chromatogr., A, 763, Turula, V. E., Bishop, R. T., Ricker, R. D. and de Haseth, J. A., Complete structure elucidation of a globular protein by particle beam liquid chromatography-Fourier transform infrared spectrometry and electrospray liquid chromatography-mass spectrometry - Sequence and conformation of /3-lactoglobulin , 91-103, Copyright (1997), with permission from Elsevier Science...
When air oxidation of the reduced p-conotoxin GIIIB (18) was carried out in 0.1 M NHtOAc buffer (pH 7.5) at 0.01 mM peptide concentration and at 10 °C, three major products, isomers 15,16, and 17 were produced after 40 hours in a ratio of 1 4 3 (Figure 2). 86 The disulfide structures of each isomer were determined by enzymatic digestion followed by amino acid analyses, mass spectrometry, sequence analyses, as well as by the synthetic approach (Scheme 10). [Pg.151]

Gouldsworthy, A. M., Leaver, J., and Banks, J. M. (1996). Application of mass spectrometry sequencing technique for identifying peptides present in Cheddar cheese. Int. Dairy ]. 6, 781-790. [Pg.205]

Chapters focus on mass spectrometry, sequence and amino acid analysis, separations, protein folding and conformation, peptide and protein NMR, and peptide synthesis. In addition, the mutagenesis and protein design section has been expanded and a new section addresses analysis of protein interactions. [Pg.607]

Koy C, Miklcat S, Raptakis E, Sutton C, Resch M, Tanaka K, Glocker MO. Matrix-assisted laser desorp-tion/ionization-quadrupole ion trap-time of flight mass spectrometry sequencing resolves structures of unidentified peptides obtained by in-gel tryptic digestion of haptoglobin derivatives from human plasma proteomes. Proteomics. 2003 Jun 3(6) 851-8. [Pg.188]

Settlage, R. E., Russo, P. S., Shabanowitz, J., and Hunt, D. F., A novel /x-ESI source for coupling capillary electrophoresis and mass spectrometry sequence determination of tumor peptides at the attomole level. J. Microcolumn Sep., 10, 281-285, 1998. [Pg.302]

Goransson, U., A.M. BromsaUs, and P. Claeson. 2003. Expression of Viola cyclotides by liquid chromatography-mass spectrometry and tandem mass spectrometry sequencing of intercyste-ine loops after introduction of charges and cleavage sites by aminoethylation. Anal. Biochem. 318(1) 107-117. [Pg.927]

Aaserud, D.J. Little, D.P O Connor, P.B. McLafferty, F.W. Distinguishing N-terminus and C-terminus ions for mass spectrometry sequencing of proteins without prior degradation. Rapid Commun. Mass Spectrom. 1995, 9, 871-876. [Pg.148]

Mass spectrometry sequencing of oligonucleotides is not as common a practice as it is for proteins and peptides. However, the following mass spectrometry-based sequence determination strategies have gained acceptance ... [Pg.464]

Thanawiroon, C., Rice, K. G., Toida, T., and Linhardt, R. J. 2004. Liquid chromatogra-phy/mass spectrometry sequencing approach for highly sulfated heparin-derived oligosaccharides. J. Biol. Ghent. 279 2608-2615. [Pg.409]

From the [M + H] peak, molecular weights of large peptides are easily obtained by FD mass spectrometry. Sequence-specific cleavages on both sides of the CO group of peptide bonds are observed, so the determination of the complete sequence of amino acids is difficult 160 see also 161). [Pg.57]

Wen DX, Livingston BD, Medzihradszky KF, Kelm S, Burlingame AL, et al. Primary Structure of Galbetal,3(4)GlcNAc 2,3-Sialyltransferase Determined by Mass Spectrometry Sequence Analysis and Molecular Cloning—Evidence for a Protein Motif in the Sialyltransferase Gene Family. 7. Biol. Chem. 1992 267 21011 21019. [Pg.1344]

Wen, D. X., Livingston, B. D., Medzihradszky, K. F., Kelm, S., Burlingname, A. L., and Paulson, J. C., 1992, Primary structure of Galpl,3(4)GlcNAc a2,3-sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning, J. Biol. Chem. 267 21011-21019. [Pg.66]


See other pages where Mass spectrometry sequencing is mentioned: [Pg.493]    [Pg.293]    [Pg.305]    [Pg.464]    [Pg.465]    [Pg.467]    [Pg.469]    [Pg.471]    [Pg.473]    [Pg.474]    [Pg.475]    [Pg.212]    [Pg.77]    [Pg.221]   
See also in sourсe #XX -- [ Pg.37 , Pg.38 , Pg.39 , Pg.43 , Pg.44 , Pg.45 ]




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