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Peptides by chromatography

Schroeder, W. A. "Separation of Peptides by Chromatography on Columns of Dowex 1 with Volatile Developers", In "Methods In Enzymology", p. 214, Vol. XXV, "Enzyme Structure, Part B", C. H. W. Hlrs and S. N. Tlmasheff, Editors, Academic Press, New York, 1972. [Pg.48]

Purify the tryptic peptides by chromatography on a C18 column to remove salts (follow the manufacturer s directions for peptide purification). Dry the eluent and redissolve the peptides in 20 pi 0.1 percent formic acid. [Pg.1016]

Careri M, Mangia A. Analysis of food proteins and peptides by chromatography and mass spectrometry. J Chromatogr A 2003 1000(l-2) 609-635. [Pg.640]

CM-cellulose chromatography analysis of tryptic peptides by chromatography and electrophoresis... [Pg.168]

Adapted from Jones, B. V., Pddbo,. S ., and. Stein,. S ., 1981. Amino aeid analysis and enzymie seqnenee determination of peptides by an improved, o-phthaldialdehyde preeolnmn labeling pro-Journal of Liquid. Chromatography 4 56—586.)... [Pg.105]

Henderson, D. E. and Mello, J. A., Physicochemical studies of biologically active peptides by low-temperature reversed-phase high-performance liquid chromatography, /. Chromatogr., 499, 79, 1990. [Pg.197]

Cutillas, P.R., Norden, A.G., Cramer, R., Burlingame, A.L., Unwin, RJ. (2003). Detection and analysis of urinary peptides by on-line liquid chromatography and mass spectrometry application to patients with renal Fanconi syndrome. Clin. Sci. (Lond.) 104, 483 490. [Pg.256]

Figure 19.8 To study the conjugation of peptides to carriers using different levels of EDC, tyrosyl-lysine was conjugated to BSA and separated after the reaction by chromatography on a Sephadex G-25 column. As the EDC level was increased in the reaction, more peptide reacted and the peptide peak (the second peak) was depleted. The absorbance of the carrier peak (the first one) increases as more peptide is conjugated. Figure 19.8 To study the conjugation of peptides to carriers using different levels of EDC, tyrosyl-lysine was conjugated to BSA and separated after the reaction by chromatography on a Sephadex G-25 column. As the EDC level was increased in the reaction, more peptide reacted and the peptide peak (the second peak) was depleted. The absorbance of the carrier peak (the first one) increases as more peptide is conjugated.
A two-dimensional technique involving initial separation by high voltage electrophoresis at pH 2.0 followed by chromatography is a useful means of separating similar amino acids and short peptides and does not require desalting or excessive purification of the sample (Figure 10.17). [Pg.370]

D Agostino PA, Hancock JR, Provost LR. 1997. Analysis of bioactive peptides by liquid chromatography-high-resolution electrospray mass spectrometry. J Chromatogr... [Pg.170]

Koezuka, K., Ozaki, H., Matsubara, N., and Terabe, S. (1997). Separation and detection of closely related peptides by micellar electrokinetic chromatography coupled with electrospray ionization mass spectrometry using the partial filling technique.. Chromatogr. B 689, 3—11. [Pg.312]

Polo, M.C., Ramos, M. and Sanchez, R. (1985). Free amino acids by high performance liquid chromatography and peptides by gel electrophoresis in Mahon cheese during ripening. Food Chem., 16, 85. [Pg.157]

Example 29 iV,Ar-diisopropyl-bis[(trimethylsilyl)ethyl]phosphoroamidite have been prepared from commercial available dichloro(diisopropy-lamino)phosphine and 2-(trimethylsilyl)-ethanol [60] in 65% yield after purification by chromatography. Chao et al. have used this phosphitylating reagent in a way which is compatible with the Fmoc/tcrt-butyl strategy for the synthesis of phosphotyrosine containing peptides [61]. [Pg.117]

Lawesson s reagent (3.56 g, 0.0088 mol) and peptide (0.005 mol) in anhyd benzene (10 mL) were stirred at 80 °C until the starting material was consumed (monitored by TLC or HPLC). The solvent was removed and the residue purified by chromatography (silica gel). Excessive Lawesson s reagent was eluted with CH2C12 and the peptide eluted with EtOAc/CH2Cl2 (9 1). The product was recrystallized (MeOH/Et20). [Pg.520]

Hydrophobic Effects and Solvophobic Considerations for the Isolation of Peptides by Reversed-Phase Chromatography Methods... [Pg.555]

Der Terrossian, E. Pradel, L.-A. Kassab, R. Desvages, G. Separation of the two non-identical subunits of lombricine kinase from Lumbricus terrestris muscle by chromatography on sepharose-mercurial. Isolation of the tryptic peptide containing its essential thiol group. Eur. J. Biochem., 45, 243-251 (1974)... [Pg.406]


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See also in sourсe #XX -- [ Pg.40 , Pg.41 ]




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